Biochemical study of collagen in adult groin hernias

被引:58
作者
Pans, A
Albert, A
Lapière, CM
Nusgens, B
机构
[1] Clin A Renard, Univ Dept Abdominal Surg, B-4040 Herstal, Belgium
[2] CHU Sart Tilman, Dept Biostat, B-4000 Liege, Belgium
[3] CHU Sart Tilman, Lab Connect Tissues Biol, B-4000 Liege, Belgium
关键词
inguinal hernia; etiology; collagen; biochemistry;
D O I
10.1006/jsre.2000.6024
中图分类号
R61 [外科手术学];
学科分类号
摘要
Background. Previous works have suggested that a defect in collagen fiber structure may play a role in inguinal hernia formation. These studies focused mainly on the rectus sheath or the skin, while only few reports dealt with the transversalis fascia. According to these findings and to our previous biomechanical and histological studies suggesting that a connective tissue pathology could play a role in the genesis of groin hernias, we performed a biochemical investigation of the collagen in the transversalis fascia and rectus sheath. Materials and Methods. The samples were collected from 40 adult patients with uni- or bilateral hernias and from 20 control subjects without hernia (autopsies and organ donors). A constant area of tissue was taken by using a calibrator. The wet and dry weights per 100 mm(2) were determined and the total collagen concentration as well as its sequential extractibility in NaCl, acetic acid, and pepsin was measured. The ratios of alpha (1)/alpha (2), chains (I) and of type I/III collagen were assessed by polyacrylamide gel electrophoresis. Results. Samples collected in the control and patient sheaths showed an increased wet weight per 100 mm2 in the patients. The wet and dry weights per unit area were increased in the patient fascias. The collagen concentration was increased in the indirect hernias. The fascias from the direct hernias (DH) presented a significantly increased collagen extractibility after pepsin digestion (5.6%), when compared to the control fascias (2.6%). The extractibility was 3.4% in the nonherniated (NH) sides. The qualitative study (ratios alpha (1)/alpha (2) (I) and I/III collagen) showed no difference between the fascia groups. Conclusions. The significant increase of collagen extractibility with pepsin in the DH fascias and at a lesser degree in the NH fascias suggests that molecular alterations of collagen could be involved in the genesis of groin hernias. This connective tissue pathology would express preferentially its effects in the inguinal region, since we have observed no major difference between the rectus sheaths of controls and those of patients. (C) 2001 Academic Press.
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页码:107 / 113
页数:7
相关论文
共 24 条
[1]   Study of biochemical substrate and role of metalloproteinases in fascia transversalis from hernial processes [J].
Bellon, JM ;
Bujan, J ;
Honduvilla, NG ;
Jurado, F ;
Gimeno, MJ ;
Turnay, J ;
Olmo, N ;
Lizarbe, MA .
EUROPEAN JOURNAL OF CLINICAL INVESTIGATION, 1997, 27 (06) :510-516
[2]   2 IMPROVED AND SIMPLIFIED METHODS FOR SPECTROPHOTOMETRIC DETERMINATION OF HYDROXYPROLINE [J].
BERGMAN, I ;
LOXLEY, R .
ANALYTICAL CHEMISTRY, 1963, 35 (12) :1961-&
[3]   METASTATIC EMPHYSEMA - A MECHANISM FOR ACQUIRING INGUINAL HERNIATION [J].
CANNON, DJ ;
READ, RC .
ANNALS OF SURGERY, 1981, 194 (03) :270-278
[4]   INCREASES IN TYPE-III COLLAGEN GENE-EXPRESSION AND PROTEIN-SYNTHESIS IN PATIENTS WITH INGUINAL-HERNIAS [J].
FRIEDMAN, DW ;
BOYD, CD ;
NORTON, P ;
GRECO, RS ;
BOYARSKY, AH ;
MACKENZIE, JW ;
DEAK, SB .
ANNALS OF SURGERY, 1993, 218 (06) :754-760
[5]  
GROSS J, 1960, P SOC EXP BIOL MED, V105, P148
[7]   SHOULDICE INGUINAL-HERNIA REPAIR IN THE MALE-ADULT - THE GOLD STANDARD - A MULTICENTER CONTROLLED TRIAL IN 1578 PATIENTS [J].
HAY, JM ;
BOUDET, MJ ;
FINGERHUT, A ;
POURCHER, J ;
HENNET, H ;
HABIB, E ;
VEYRIERES, M ;
FLAMANT, Y .
ANNALS OF SURGERY, 1995, 222 (06) :719-727
[8]  
KLINGE U, 1999, HERNIA, V4, P181
[9]   CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].
LAEMMLI, UK .
NATURE, 1970, 227 (5259) :680-+
[10]  
LAMBERT CA, 1992, LAB INVEST, V66, P444