The How, When, Where and Why of Hernia - advances in prevention and cure.
Posted on August 09 2021
Now here’s some alarming statistics.
- Worldwide, more than 20 million patients undergo groin hernia repair annually.(1)
And In Australia,(2)
- Between the years 2000 and 2015, a total of 324 618 groin hernia repairs were performed on adult patients, 43% by a laparoscopic method.
- Approximately 40,000 Australians have their hernias surgically repaired every year
- An estimated 1 in 4 men and 1 in 50 women will require surgery for a hernia during their lifetime.
But my guess is you are not reading this because you’re interested in statistics.
You’re probably reading this because you have a hernia yourself or you know someone close to you who does, and you’re looking for answers. Well read on because in this article we reference over 30 scientific studies and highlight the very latest cutting-edge science and innovative health supplements providing exciting advances in prevention and cure.
So, what Is a Hernia?
A hernia is the protrusion of organs, such as intestines, through a weakened section of the abdominal wall. If left untreated, the split in the muscle widens and greater amounts of tissue or organs are pushed through the opening, forming a sac. This visible lump or bulge is one of the key characteristics of a hernia.
Inguinal hernias are located in the lower abdomen just above the leg crease, near or adjacent to the pubic area. They can sometimes occur on both sides of the pubic area, and if they do, they are called bilateral inguinal hernias. Inguinal hernias, along with femoral hernias make up the 2 types of groin hernias and can produce pain that extends into the upper thigh or scrotum.
Inguinal hernias can be classified as “direct” or “indirect”.
- An indirect inguinal hernia occurs through the natural weakness in the internal inguinal ring.
- A direct inguinal hernia is a result of weakness in the floor of the inguinal canal and is more likely to develop in older men over the age of 40.
A Sportsman's Hernia is a condition of chronic exercise-related groin pain. Generally, it involves a direct inguinal hernia. Symptoms are pain in the groin without any detectable swelling in the groin or any other explanation for the pain.
Femoral hernias, along with inguinal hernias are groin hernias. They are much more common in women but can occur in men. These hernias appear just below the groin crease. A weakness in the lower groin allows an intestinal sac to drop into the femoral canal, a space near the femoral vein that carries blood from the leg. These hernias are more prone than inguinal hernias to develop incarceration or strangulation as an early complication.
A hernia that appears in the abdomen at the site of a previous surgery is known as an incisional hernia. These hernias can appear weeks, months, or even years after surgery and can vary in size from small to very large and complex.
Epigastric and Ventral hernias are more common in men than women. They occur due to a weakness, gap, or opening in the muscles or tendons of the upper abdominal wall, on a line between the breast bone and the navel or umbilicus.
Spigelian Hernia is a protrusion of intestine or an empty sac through a weakness between the muscle fibers of the abdominal wall, often on the right-hand side of the abdomen. Often there is no obvious swelling or lump, so it can make it almost impossible to detect. It develops between the muscles of the abdominal wall rather than protruding through layers of fat. It may be mistaken for another type of abdominal complaint. This is quite a rare type of hernia which occurs in both male and females. It often develops in later life when the abdominal muscles have become weaker.
If the hernia resists manual pressure and can’t be popped back through the abdominal wall, it is known as a non-reducible hernia. This means that the intestinal loop is held tight by the muscular ring, which can lead to further swelling of the loop and eventual strangulation of the entrapped bowel. The femoral hernia is the most susceptible to this complication.
Symptoms of a strangulated hernia include nausea, vomiting and severe pain. Prompt medical attention and surgery is vital. Untreated, a strangulated hernia can lead to gangrene of the trapped bowel.
Both reducible and non-reducible hernias need to be surgically repaired. The various procedures used depend on the location of the hernia, but may include opening the abdomen and using stitches and nylon meshes to close and reinforce the weakened section of muscle. Inguinal hernias can be repaired using laparoscopic surgery.
Advances In Hernia Research
Despite technical developments over the last 3 decades, population-based analyses have revealed no pronounced reduction in recurrence rates.
This somewhat surprising finding gives rise to a new concept of hernia biology that puts forward the premise that disturbances in collagen metabolism contribute to hernia disease and high recurrence rates.
Studies focusing on hernia as a disease of the extracellular matrix (ECM) reflect a new approach to decipher the biology of recurrent or direct inguinal hernia and incisional hernia formation.
The ECM is the non-cellular portion of a tissue. It is a collection of extracellular material produced and secreted by cells into the surrounding medium. The main function of the ECM is to provide structural and biochemical support to the surrounding cells.
Our connective tissue supports many different parts of our body, such as our skin, eyes, and heart. It is like a "cellular glue" that gives our body parts their shape and helps keep them strong. It also helps some of our tissues do their work. It is made of many kinds of proteins, predominantly collagen.
Collagens are a large family of triple helical proteins that are found throughout our entire body. They have a broad range of functions, including cell adhesion, cell migration, tissue morphogenesis, tissue scaffolding, and tissue repair. Collagens are abundant in ligaments, tendons, cartilage, and in muscle as fibrillar proteins, and not only give structural support to resident cells, but also regulate the resident and inflammatory cell function. Collagen fibres are imbedded in ECM, and undergo a continuous process of synthesis and degradation under the action of matrix metalloproteinases (protein enzymes).
Collagen has mechanical properties sufficient to enable it to support healed scars and other tissues. Over 20 distinct types of collagens have been recognized, the most common of which are Types I and III. Type I predominates as healing proceeds whereas Type III collagen is the second most abundant collagen of soft tissues and dominates early phases of wound healing.
Many scientists are now studying the role of collagen in hernia and have even defined hernia as a disease of the ECM!
It is now suggested that inguinal hernia is not so much a local disease as it is a local manifestation of a systemic disorder of collagen metabolism. Numerous studies are showing that patients with inguinal hernia have some anomalies in collagen metabolism and a changed ratio of collagen types.
These studies have revealed marked changes in the abundance, composition, and metabolism of interstitial collagens in patients with recurrent hernia diseases, adult groin hernia and incisional hernia. These observations have led to the suggestion that hernia formation and the recurrence of incisional hernia may be explained by disordered tissue renewal and by abnormal wound healing, respectively.
Results of studies (3) conducted as early as 1970 indicated that in inguinal herniation the rectus sheath is thinner than normal. The study shows that a deteriation in the sheet-like facia that joins muscle to other body parts explains the development and recurrence rate of inguinal herniation in adults.
Since then, other studies (4), (5), (6) have confirmed that, in abdominal aortic aneurysm patients, a genetic predisposition to the formation of abdominal wall hernias was also suggested. The finding supports the long-held impression of a common ECM defect in both vascular wall and abdominal wall collagen metabolism.
The Collagen-Hernia Connection
But it was in 1982, when Busuttil (7) a vascular surgeon now renowned for transplantation, reported that the Type I to Type III collagen ratio was decreased in the aortic media of patients with abdominal aortic aneurysm (a balloon-like bulge in the aorta, the large artery that carries blood from the heart through the chest and torso).
More and more studies confirm this collagen imbalance, with Scientists now suggesting that the presence of a high quantity of collagen Type III in the tissue obtained from cases operated for hernia, indicates that there is an intrinsic and inherent weakness in the tissue which makes the individual more prone for developing primary, incisional or recurrent hernias.
More recent studies (8) (9) have proved that ventral, recurrent and primary inguinal hernias are not just caused because of a primary defect but an acquired disorder with respect to collagen distribution.
This study (10) confirmed previous findings of a significant increase of synthesis of Type III collagen, and also show a similar fall in the Type I / Type III ratio. This index has emerged as a possible tool for determining in any adult with abdominal herniation whether connective tissue disease is present and to what degree.
Results of this study (11) by Antonio Britto Casanova et al. published in the American Journal of Surgery, showed 17.3% less total collagen in patients with hernias compared with the control group. Type I collagen in patients with indirect inguinal hernias was 23.7% less than the control group, type III collagen was 6.4% less in the controls. The study concluded that the lower percentages of total collagen and type I collagen in the transversalis fascias (the thin layer of connective tissue lining most of the abdominal cavity) of patients with indirect inguinal hernias could be a factor in hernia formation.
This study (12) demonstrated that there was a significant lesser amount of collagen and higher amounts of elastic fibres in transversalis fascia from those patients with direct inguinal hernia as compared to those patients with indirect inguinal hernia.
A study by Henriksen NA (13) showed a significant increase in the immature collagen type III with relation to the stronger collagen type I in those patients with a hernia, which further resulted in thinner collagen fibres with a decreased biomechanical strength. A consistent finding was a significant increase in immature type III collagen relative to the stronger type I collagen in patients with a hernia. This resulted in thinner collagen fibres with a correspondingly diminished biomechanical strength. It has been suggested that these alterations are due to variation in the synthesis, maturation or degradation of collagen by matrix metalloproteinases, in combination or alone. The study concluded that hernia formation and recurrence is associated with altered collagen metabolism manifested by a decreased type I:III collagen ratio.
Wagh et al.(14) suggested that diminished collagen, in the sheath of the rectus abdominis muscles of patients causes indirect or direct inguinal hernias. They studied the amount of collagen and elastic fibers in the transversalis fascia of 36 male patients with indirect inguinal hernia and 21 with direct inguinal hernia. They were able to demonstrate significantly lower amounts of collagen and higher amounts of elastic fibers in transversalis fascia from patients with direct inguinal hernia compared to indirect inguinal hernia patients. The transversalis fascia from direct inguinal hernia patients showed structural changes of the mature and elaunin elastic fibers, which are responsible for elasticity, and lower density of oxytalan elastic fibers, which are responsible for resistance. These changes promoted loss of resiliency of the transversalis fascia.
The study (15) showed that in patients with inguinal hernia, there are less collagen in the hernia's wall. The authors also noticed the thickness of transversalis fascia from hernia patients were 58% thinner than those of the control. They concluded that the direct inguinal hernia patients have less collagen in transversalis fascia either absolutely or relatively to other constitutional elements.
These observations indicated that inguinal herniation in the adult could be related to reduced collagen synthesis by fibroblasts, presumably leading to a weakening of the transversus abdominis aponeurosis and transversalis fascia. All of the changes observed were much more marked in those individuals presenting with direct herniation as opposed to the indirect type.
Finally, this meta study published in 2016 (16), reviewed 61 published medical articles which revealed that multiple authors suggest a qualitative or quantitative defect in collagen formation as a common factor in hernia formation, and this trend in pathologic studies suggests a link between abnormal collagen production and/or processing that is likely associated with hernia development.
So What Is Type I and Type III Collagen?
Collagen is our predominant structural protein, especially of abdominal wall fascial layers, comprising 80% or more of structural tissue. It can be found abundantly in organs such as bones, the liver, kidney, heart, teeth, our muscles, tendons, ligament and skin. Collagen provides the necessary structural framework for tissues in which it is found. It also helps the development of the organs, wound and tissue healing, cornea, gums, and scalp repair. Collagen helps in bone and blood vessel reparation. It is present in biological functions of the cell such as proliferation, cell survival, and differentiation.
Collagen is also the principal component of the ECM. Type I and III are the most predominant, and comprise 95% of the whole. They interact to form the bundle architecture. Type I are strong and big, whereas Type III are thin and flexible. Normally, the former are approximately four times as prevalent as the latter. Type III collagen is believed to accommodate the expansion and contraction of tissues such as blood vessels and viscera, (the internal organs in the main cavities of the body, especially those in the abdomen, e.g. the intestines).
Collagen type I is the most common in skin, bone, teeth, tendon, ligaments, vascular ligature, and organs. It comprises about 80% of dermal collagen and plays a major role in providing tensile strength to skin. It is the predominant collagen in mature tendons and ligaments, where it gives them their load-bearing mechanical properties.
However, if there are any alterations in the delicate balance of collagen types in the extracellular matrix, then problems arise. Increasing collagen I:III ratio would provide additional rigidity to tissue structure, whereas decreasing this ratio would provide elasticity and flexibility to the tissue. The proper function of tissues is reliant on this scale not tipping too far in either direction.
Defects result in either delayed or abnormal collagen synthesis or increased wound protease activity leading to collagen degradation. The result is an imbalance in repair collagen homeostasis leading to a reduction in wound collagen levels, wound tensile strength and an increased risk of mechanical wound failure.
The Role of Proline, Hydroxyproline, and Arginine
The amino acid, hydroxyproline (HYP), is a major component of collagen, and plays a key role in the stability of the collagen triple helix. Approximately 99.8% of the body's stores of HYP are found in collagen. HYP levels are measured as a marker for total collagen deposition and have shown to be substantially reduced in patients with hernia.
In this study (17), scientists measured the structural tissues of patients with inguinal hernias and found they had a significant reduction in their levels of hydroxyproline and collagen. They noted that Isolated fibroblasts from these patients expressed a proliferative defect and a reduced ability to translocate hydroxyproline.
Another amino acid found in collagen, Proline, is significantly lower in rectus sheath samples taken from patients with hernia as opposed to those without. This study (18) showed there is a relationship between proline levels with age, and onset of incidence among indirect inguinal hernia.
Arginine (ARG), a semi-essential amino acid, plays a fundamental role in the metabolism of various body components, displaying numerous and peculiar pharmacological effects. It is recruited in the acute and chronic phases of healing and it is a precursor, among other molecules, of nitric oxide (NO), which favours angiogenesis and the healing process as a whole. Angiogenesis (the formation of new blood vessels) is a healing phenomenon of the proliferative phase that occurs so that cells and growth factors can continue the remodeling phase, with collagen maturation and increased tensile strength.
In humans, ARG is synthesized in adequate quantities to sustain muscle and connective tissue mass but probably in insufficient quantities for optimal collagen biosynthesis and healing following injury. In situations of stress or injury, body stores of ARG decrease rapidly. It is during these times, in which endogenous synthesis is insufficient to meet the demands of increased protein turnover, that ARG becomes an indispensable amino acid for wound healing and the maintenance of a positive nitrogen balance.
Arginine has been shown to enhance wound strength and collagen deposition in artificial incisional wounds in rodents and humans. A role for dietary intervention in the form of arginine supplementation has been proposed to normalize or enhance wound healing in humans (19).
This study (20) showed that in the abdominal wall healing evaluation of Wistar rats under arginine treatment, there was an increase in type I collagen maturation, microvascular density and improvement in scar granulation tissue formation.
Arginine supplements influence growth and healing of skin incisional wounds. This study (21) concluded that arginine is essential for the synthesis of the increased amounts of reparative collagen required for wound healing, and it decreases some of the negative aspects of the metabolic responses to injury and improves wound strength.
The best method to support wound collagen biosynthesis is by providing adequate host nutrition. ARG supplementation is most effective in increasing collagen deposition. Experts advise that the best source of Hydroxyproline, Proline, and Arginine is to supplement with Hydrolysed Collagen powder with the three containing over 20% of its whole.
Skin as a Marker for Collagen Ratio
Friedman et al (22) 1993 described a change in cultured fibroblasts obtained from the skin of patients with inguinal herniation. His team concluded that the presence of such a change would render an individual liable to herniation, incisional breakdown, and reoccurrence. This study was the first attempt which showed the world that individuals with the abnormality in the collagen production have a higher chance for developing hernias.
This study (23) published in 1999 indicated that the ratio of collagen type I/III was significantly decreased in the skin of patients with either indirect or direct hernia, with a concomitant increase in collagen type III vs. controls. The authors concluded that the decreased ratios of collagen type I/III could be of significant importance for the pathophysiology of hernias. The specific ratio collagen I/III probably reflects the altered structural integrity and mechanical stability of the connective tissue in both indirect and direct hernias.
The decreased tensile strength of collagen type III plays a key role in the development of incisional hernias (24). The data from the 2002 study confirmed that the presence of incisional hernia is accompanied by impaired collagen synthesis in the skin. Again confirming that the decreased tensile strength of collagen type III may play a key role in the development of incisional hernias. Not only that, but it might explain the high recurrence rates of hernia repair by simple closure, as a repetition of the primarily failing technique, and the improvement by the additional use of alloplastic material.
A study by Peeters, DeHertogh, Junge, in 2014, (25) compared the collagen type I/III ratio in patients with primary inguinal, recurrent inguinal, primary incisional and recurrent incisional hernia with controls and demonstrated that the ratio was significantly lower in skin and anterior rectus sheath fascia of the cases and also showed that incisional and recurrent inguinal hernia had lower ratio than primary inguinal hernia patients. And the important point noticed was that collagen type I/III ratio in skin was representative for that in abdominal wall fascia.
Does Collagen Improve Scar Tissue?
In this study (26) scientists found that patients with recurring hernias exhibited a significantly decreased ratio of Type I collagen to Type III. They concluded that the composition of scar tissue with a lowered collagen type I/III ratio and therefore, reduced tensile strength, may be a major contribution to hernia recurrence.
In this study (27), skin scars from patients with either primary or recurrent incisional and recurrent inguinal hernias, were analyzed for overall collagen content and for the distribution of collagen types I and III. They found that patients with recurrent incisional hernia showed lowest ratios of collagen types I to III. The expression of tenascin (an adhesion-modulating extracellular matrix protein) was notably decreased in all hernia groups. They concluded that the observed alterations in the expression of collagen-interacting proteins again indicate the possibility of a fundamental connective tissue disease as the causal factor in the pathogenesis of (recurrent) incisional hernias.
It is the pathological changes in collagen that set the stage for the development of a hernia.
New Theories in Hernia Repair and Prevention
The causes of hernias are multi factorial, the components of the extracellular matrix, and the importance of collagen which promote a loss of resistance and elasticity of the transversalis fascia determines the onset and recurrences of hernias.
In Australia, leaders in hernia surgery are now recommending their patients ingest marine collagen powder pre and post operation as studies (28) have shown a transient increase in collagen-derived peptides, especially of Pro-Hyp, in the blood and skin after ingestion of collagen hydrolysate.
Collagen hydrolysate, a well-known nutritional supplement for the improvement of healthy skin, consists of small peptides with low molecular weight. Due to its low molecular weight, hydrolysed collagen is easily digestible, absorbed and distributed in the human body.
When administered orally, hydrolysed collagen reaches the small intestine where it is absorbed into the blood stream, both in the form of small collagen peptides and free amino acids. Through the network of blood vessels, these collagen peptides and free amino acids are then distributed in the human body, in particular to the dermis, where it has been proven they can remain up to 14 days. In the dermis, hydrolysed collagen has a dual action mechanism: 1) free amino acids provide building blocks for the formation of collagen and elastin fibres; 2) collagen oligopetides act as ligands, binding to receptors present on the fibroblasts’ membrane and stimulate the production of new collagen, elastin and hyaluronic acid.
What is Hydrolysed Collagen Supplementation Effects on Wound Healing?
Addressing the innate collagen deficit through collagen supplementation offers a promising strategy to restore ECM homeostasis and aid cutaneous wound healing. To this aim, there has been increased interest in the use of orally administered nutraceutical collagen peptides derived from animal skin collagen, constituting a mixture of low-molecular-weight, water-soluble peptides that are rich in amino acids such as hydroxyproline, glycine, arginine, and proline.
Pro-Hyp is a low molecular weight growth-initiating factor for specific fibroblasts that is involved in the wound healing process. Pro-Hyp is also supplied to tissues by oral administration of gelatin or collagen hydrolysate. Thus, supplementation of gelatin or collagen hydrolysate has therapeutic potential for chronic and incisional wounds. Animal studies and human clinical trials (29) have demonstrated that the ingestion of gelatin or collagen hydrolysate enhances the healing of pressure ulcers in animals and humans and improves delayed wound healing in diabetic animals. Therefore, the low molecular weight fibroblast growth-initiating factor, Pro-Hyp, plays a significant role in wound healing and has therapeutic potential for chronic wounds.
This study (30) was designed to investigate the effect of marine collagen peptides on wound healing and angiogenesis in rats. 96 animals were randomly treated with marine collagen peptides. Wound closure and tensile strength were calculated. The results showed that hydrolysed collagen reduced matrix metalloproteinase-1 production (the enzyme that degrades collagen), and increased the synthesis of type 1 procollagen. The plasma concentrations of Gly-Pro and Pro-Hyp increased dramatically. The rats treated with marine collagen peptides showed quicker wound closure and better tissue regeneration at the wound site. Moreover, marine collagen peptides treatment improved angiogenesis and contributed in forming a thicker and better organised collagen fiber deposition when compared to the control group.
These studies show that the structural and mechanical properties of collagen within the ECM are key to tissue integrity. Addressing the innate collagen deficit within aged skin through collagen supplementation therefore offers a promising strategy to restore ECM homeostasis and aid cutaneous wound healing.
So the benefits from ingestion of collagen powder may be threefold. 1. Improving the ratio of Type I to Type III collagen in the body; 2. Increasing the healing time of wounds; and 3. improving the strength of scar tissue.
So Which Hydrolysed Collagen is Best?
The study published in the Journal of Clinical and Experimental Dermatology in 2020, uses CollagenX Hydrolysed Collagen Powder and demonstrates that collagen peptides significantly increase wound closure rates in both young and aged fibroblasts. These results corroborate previous studies revealing enhanced fibroblast proliferation through the addition of prolyl-hydroxyproline-containing collagen peptides.
The use of Collagenx hydrolysates as food or dietary supplements for the improvement of skin, joint, and bone health properties is increasing. CollagenX hydrolysed marine collagen powder is a fish-derived type I collagen hydrolysate that has a unique amino acid profile that constitutes high amounts of Proline, Hydroxyproline and Alanine.
So the new frontiers of science and cutting-edge health supplementation may just be providing the good news all hernia suffers have been waiting for.