Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Collagen Type I”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1995

Increased expression of messenger RNA for collagen type I, collagen type III, and fibronectin in myometrium of pregnancy.

OBJECTIVE: To determine the expression of the extracellular matrix proteins collagen type I, collagen type III, and fibronectin by immunohistochemistry, and the messenger RNA (mRNA) for these proteins by Northern blot analysis in the myometrium of pregnancy compared with myometrium from normal premenopausal women. METHODS: Myometrial tissue was obtained from seven pregnant women undergoing elective cesarean delivery and eight nonpregnant premenopausal women undergoing hysterectomy. Tissue was paraffin embedded and processed for RNA. Antibodies to collagen type I, collagen type III, and fibronectin were used to examine protein expression by immunohistochemistry. Complimentary DNA probes for the same proteins were used to examine mRNA expression by Northern blot analysis. RESULTS: Increased staining was seen for all three proteins in the myometrium of pregnancy. Densitometric analysis of Northern blots showed increased levels of collagen type I mRNA (P < .003), collagen type III mRNA (P < .005), and fibronectin mRNA (P < .04) in the myometrium of pregnancy compared with myometrium from nonpregnant premenopausal women. CONCLUSION: There is increased expression of both protein and mRNA for collagen type I, collagen type III, and fibronectin in the myometrium of pregnancy.

Blotting, Northern↗
PubMed2004

Early and stable upregulation of collagen type II, collagen type I and YKL40 expression levels in cartilage during early experimental osteoarthritis occurs independent of joint location and histological grading.

While morphologic and biochemical aspects of degenerative joint disease (osteoarthritis [OA]) have been elucidated by numerous studies, the molecular mechanisms underlying the progressive loss of articular cartilage during OA development remain largely unknown. The main focus of the present study was to gain more insight into molecular changes during the very early stages of mechanically induced cartilage degeneration and to relate molecular alterations to histological changes at distinct localizations of the joint. Studies on human articular cartilage are hampered by the difficulty of obtaining normal tissue and early-stage OA tissue, and they allow no progressive follow-up. An experimental OA model in dogs with a slow natural history of OA (Pond-Nuki model) was therefore chosen. Anterior cruciate ligament transection (ACLT) was performed on 24 skeletally mature dogs to induce joint instability resulting in OA. Samples were taken from different joint areas after 6, 12, 24 and 48 weeks, and gene expression levels of common cartilage molecules were quantified in relation to the histological grading (modified Mankin score) of adjacent tissue. Histological changes reflected early progressive degenerative OA. Soon after ACLT, chondrocytes responded to the altered mechanical conditions by significant and stable elevation of collagen type II, collagen type I and YKL40 expression, which persisted throughout the study. In contrast to the mild to moderate histological alterations, these molecular changes were not progressive and were independent of the joint localization (tibia, femur, lateral, medial) and the extent of matrix degeneration. MMP13 remained unaltered until 24 weeks, and aggrecan and tenascinC remained unaltered until 48 weeks after ACLT. These findings indicate that elevated collagen type II, collagen type I and YKL40 mRNA expression levels are early and sensitive measures of ACLT-induced joint instability independent of a certain grade of morphological cartilage degeneration. A second phase of molecular changes in OA may begin around 48 weeks after ACLT with altered expression of further genes, such as MMP13, aggrecan and tenascin. Molecular changes observed in the present study suggest that dog cartilage responds to degenerative conditions by regulating the same genes in a similar direction as that observed for chondrocytes in late human OA.

Adipokines↗
PubMed1991

Human bone contains type III collagen, type VI collagen, and fibrillin: type III collagen is present on specific fibers that may mediate attachment of tendons, ligaments, and periosteum to calcified bone cortex.

We evaluated the distribution of Type III collagen, Type VI collagen, and fibrillin in human bone, using monoclonal antibodies (MAb) of proven specificity. All three molecules are present in developing and remodeling bone. Type III collagen is present in discrete fiber bundles throughout the bone cortex but is concentrated at the Haversian canal surface and in the fibers at the bone-periosteal interface. The collagen fibrils in these bundles are of uniform diameter. Type III-containing collagen fibers are detected at all ages examined, from 30 fetal weeks to 80 years. Type VI collagen is present in fetal bone in discrete fibrils separate from Type III collagen, and becomes restricted to the margins of bone cells and the bone surface by 7 years. The distribution of fibrillin resembles that of Type III collagen in the fetus, but at 7 years is absent from the interior of the cortex except for the canaliculi and cement lines, and remains concentrated in discrete fibers at the bone surface.

Adult↗
PubMed1989

Distribution of laminin, collagen type IV, collagen type I, and fibronectin in chicken cardiac jelly/basement membrane.

Light microscopic immunolabeling studies were designed to identify and locate structural components within the cell-free extracellular matrix which lies between the embryonic endocardial and myocardial tubes. Affinity-purified antibodies were used to examine stage 15-22 embryonic chicken hearts. Specimens were immunolabeled by using three different methodologies: 1) postembedding labeling of 10 microns cryostat sections, 2) preembedding labeling (en bloc) of whole hearts, and 3) postembedding labeling of ethanol/acetic acid-fixed paraffin sections. Our results establish the spatial distribution of collagen type I and demonstrate for the first time the presence of collagen type IV and laminin in the myocardial-basement-membrane/cardiac jelly.

Animals↗
PubMed1999

Platelet adhesion to collagen type I, collagen type IV, von Willebrand factor, fibronectin, laminin and fibrinogen: rapid kinetics under shear.

Extracellular matrix proteins in the blood vessel wall fulfill an essential role in haemostasis by promoting platelet adhesion at the site of vessel injury. We have combined a continuous-flow system with affinity chromatography to study platelet adhesion under conditions mimicking arterial flow and have examined the adhesion kinetics of unstimulated platelets to collagens type I and IV, von Willebrand factor (vWf), fibronectin, laminin and to fibrinogen. In the absence of red cells, in ACD-prepared plasma adhesion to collagens type I and IV or vWf was rapid, efficient (>50% in <1 s ) and independent of shear rates from 650 to 3400 s(-1) with kinetics following an inverse exponential decay curve. We introduced a simple mathematical model in which this type of kinetics arises, and which may be more generally applicable to various adhesion processes under flow conditions. The model is characterized by the rate of platelet deposition on the adhesive surface being proportional to the number of platelets in the flow. Adhesion to fibronectin was independent of shear rate, but revealed a lag phase of approximately 1.5 s before significant adhesion began. Laminin and fibrinogen supported efficient adhesion at low shear rates (650-1000 s(-1)), but a lag phase of approximately 1.5 s was seen at high shear rates (1700-3400 s(-1)). Control proteins (albumin and gelatin) supported minimal adhesion. Nonspecific adhesion to poly-L-lysine differed from that to other substrate proteins in that the kinetics were linear. In conclusion, human platelets adhered specifically, rapidly (within seconds) and efficiently to several proteins under flow conditions and the kinetics of adhesion depended on the protein serving as substrate as well as on shear rate.

Blood Platelets↗
PubMed1988

Premature rupture of fetal membranes changes in collagen type.

Collagen from the chorioamnion units from premature and term pregnancies was solubilized by limited pepsin digestion and subjected to SDS-PAG electrophoresis. Collagen types were quantitated by densitometry. It was found that collagen type III decreases and collagen type V tends to increase as gestational age advances. Investigating the relative abundance of collagen types at various membrane sites from term pregnancies revealed that type V decreases in the amnion as the rupture site is approached. It is concluded that since type V collagen is more resistant to collagenases, its decrease may predispose that particular site to rupture.

Amnion↗
PubMed2006

Mass spectrometric analysis of enzymatic digestion of denatured collagen for identification of collagen type.

Collagen type II and I from bovine were thermally denatured and digested with trypsin. The digest mixture was analyzed with liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS). Peptides in the digest mixture were identified by mass spectrometry/mass spectrometry (MS/MS) sequencing. The results indicated that the digest mixtures of collagen type II and I contained lots of specific peptides and common peptides. Specific peptides could be used as index for identifying collagen type. Articular cartilage from bovine was pretreated and analyzed with the same method to determine the collagen types. The result indicated that the method developed was effective for identification of collagen types. The research provided a possible approach for collagen identification in particular tissues.

Animals↗
PubMed1994

Distribution of procollagen type III, collagen type VI and tenascin in oral submucous fibrosis (OSF).

The distribution of procollagen type III, collagen type VI and tenascin was studied in biopsy specimens from the buccal mucosa of 19 Indian women with confirmed oral submucous fibrosis (OSF) using the immunogold-silver staining technique. Immunohistochemistry revealed a loss of stainable procollagen type III and collagen type VI in the fibrotic zones of oral submucous fibrosis compared to normal oral mucosa. Tenascin was noted only very faintly at the subepithelial basement membrane. The present study showed that procollagen type III and collagen type VI in OSF were expressed in a specific pattern which allows a clear differentiation between fibrotic areas and adjacent apparently normal connective tissue stroma. Loss of procollagen type III, and therefore a probable predominance of collagen type I in collagen fiber bundles, and an almost complete loss of collagen type VI might explain the stiffness of the oral mucosa in patients with OSF. The immunohistochemical findings provided evidence that the process of fibrosis starts in the deeper subepithelial connective tissue stroma and not close to the subepithelial basement membrane. Further studies are required to determine whether OSF is due to increased or altered synthesis and deposition of extracellular matrix proteins, altered fibrolysis or both.

Adult↗
PubMed1997

Modulation of collagen gene expression by cytokines: stimulatory effect of transforming growth factor-beta1, with divergent effects of epidermal growth factor and tumor necrosis factor-alpha on collagen type I and collagen type IV.

Transforming growth factor-beta1 (TGF-beta1) is well recognized as a potent mediator of both fibrillar (collagen type I) and basement membrane (collagen type IV) production. However, tissue injury is characterized by the concomitant expression of many cytokines and/or growth factors in addition to TGF-beta1, and the ultimate extent of extracellular-matrix (ECM) deposition may reflect the interacting effects of TGF-beta1 and these other cytokines and/or growth factors. We, therefore, sought to determine whether other cytokines and/or growth factors, known to be produced after tissue injury, are capable either alone or in combination with TGF-beta1 of modulating collagen gene expression. Collagen type I and collagen type IV gene expression was assessed in NIH-3T3 cells, a murine fibroblast-like cell line that responds to TGF-beta1, with increases in both collagen type I and collagen type IV production. TGF-beta1 coordinately induced production of collagen type IV messenger ribonucleic acid (mRNA) to a level 3.8-fold above its baseline value (p < 0.001) and collagen type I mRNA to a level 2.6-fold above its baseline value (p < 0.001). Of the other cytokines and/or growth factors tested, only epidermal growth factor (EGF) had significant effects on collagen mRNA expression. We report the novel observation that EGF significantly induced collagen type IV mRNA (3.0-fold; p < 0.001) but did not alter collagen type I mRNA expression. Platelet-derived growth factor (PDGF), basic fibroblast growth factor (bFGF), tumor necrosis factor-alpha (TNF-alpha), interleukin-1 (IL-1), and insulin-like growth factor-1 (IGF-1) did not alter the expression of mRNA for collagen type IV or collagen type I. Addition of TGF-beta1 to cytokine- and/or growth factor-treated cells increased both collagen type IV and collagen type I mRNA levels. However, collagen type IV mRNA levels were similar in cultures given TGF-beta1 alone and cultures given TGF-beta1 with other cytokines and/or growth factors; there were no additive, synergistic, or antagonistic effects after coadministration of TGF-beta1 and other cytokines and/or growth factors. With regard to collagen type I mRNA expression, all cytokines and/or growth factors tested, with the exception of TNF-alpha, had no effect on collagen type I mRNA levels in TGF-beta1-treated cultures. Importantly, TNF-alpha antagonized the stimulatory effect of TGF-beta1 on collagen type I mRNA levels. These observations support a dominant role for TGF-beta1 in stimulating coordinate expression of collagen type I and collagen type IV mRNAs by NIH-3T3 cells; EGF and TNF-alpha are capable of inducing divergent expression of the genes for these two types of collagen.

3T3 Cells↗
PubMed1993

Beta 1 integrins mediate chondrocyte interaction with type I collagen, type II collagen, and fibronectin.

Chondrocytes isolated from the cephalic region of sterna from 14-day-old chick embryos used beta 1 integrins and required either Mg2+ or Mn2+ for attachment to plates coated with type I collagen, type II collagen, and fibronectin. beta 1 integrin was concentrated in adhesion plaques of the chondrocytes plated on type I collagen, type II collagen, and fibronectin substrates. Chondrocytes expressed at least 3 alpha-subunits, including alpha 3, alpha 5, and putative alpha 2. alpha 5, but not alpha 3, had a higher molecular weight in chondrocytes than in fibroblasts. Levels of alpha 3 and alpha 5 were about 25-30% of that in fibroblasts. When the chondrocytes were cultured in the presence of ascorbate in suspension, the cells aggregated into clusters. This aggregation was dependent on beta 1 integrin and type II collagen.

Amino Acid Sequence↗
PubMed1998

Equine laminitis basement membrane pathology: loss of type IV collagen, type VII collagen and laminin immunostaining.

Disintegration of the basement membrane (BM) of the equine hoof lamellae and failure of the BM to remain attached to the basal cells of the secondary epidermal lamellae (SEL) is one of the earliest pathological events to occur in acute laminitis. Changes in the lamellar basement membrane were investigated by immunolabelling the key structural components of the BM, type IV collagen, type VII collagen and laminin in the lamellar BM of horses 48 h after the induction of laminitis. Lamellar tissues were harvested from 2 normal horses and 2 horses with acute laminitis. Immunostaining with antibody raised against human epitopes for type IV collagen, type VII collagen and laminin successfully stained the basement membranes of horse hoof lamellar tissues. Vascular tissue did not immunostain with type VII collagen antibody. Normal BM stained as a fine dark brown line and the lamellar BM was adhered to the basal cells of the SELs with no evidence of lamellar separation. At least 2 changes to the lamellar BM occurred in acute laminitis: loss of attachment of lamellar epidermal basal cells to their underlying BM and disintegration of the lamellar BM. In some sections from feet affected by acute laminitis, there was widespread separation of the SELs from their BM without loss of BM immunostaining and in others there was extensive loss of BM immunostaining. In lesions characterised by lamellar separation, the epidermal basal cells at the tips of the primary epidermal lamellae appeared to have slipped away from their BM and were an amorphous clump of epidermal cells devoid of immunostained BM. The BM from which they had separated remained in its original position in the dermis and was clearly outlined by all 3 antibodies. In other areas, however, virtually all the BM immunoreactivity at the PEL tips was absent. Only the occasional distorted SEL tip and fragments of BM retained sufficient immunostaining to allow anatomical identification. Numerous polymorphonuclear leucocytes (PMNs) invariably surrounded the tips of lamellae showing large scale loss of immunoreactivity and many PMNs had penetrated the lamellar BM and were within the epidermal compartments. PMNs were less frequent in the midlamellar region. Immunostaining of the BM of many SELs was absent in the midlamellar region. In some lamellae loss of BM immunostaining had occurred only at the bases of the SELs and fragments of immunostained BM were present in the zones of lysed BM suggesting that BM lysis was incomplete at the time of tissue fixation. In other lamellae, lysis of the BM was complete; there was no immunostained BM between SELs and the bulk of the epidermal cells of each PEL were an amorphous column of cells on either side of the central keratinised axis of the PEL. The lamellar BM which remained appeared as immunostained strands of unattached BM along the edges of the PDLs. Activation of BM degrading metalloproteinases (MMPs) occurs in acute laminitis and it seems likely that uncontrolled MMP activity is responsible for the loss and disorganisation of lamellar BM demonstrated in this study.

Acute Disease↗
PubMed2004

Phenotypic expression of collagen type II and collagen type I gene in monolayer culture of human auricular chondrocytes.

Cartilage is regularly needed for reconstructive surgery. Basic research in tissue engineering is necessary to develop its full potential. We presented here the expression profile of type II collagen gene and type I collagen gene in human auricular monolayer culture expansion. Cultured chondrocytes documented a reduction in the expression level of collagen type II gene whilst collagen type I gene was gradually expressed through all the passages. This study demonstrated that human auricular chondrocytes lose its phenotypic expression during monolayer culture expansion. Further studies are required to enhance cartilage specific gene expression, collagen type II throughout the in vitro culture.

Cells, Cultured↗
PubMed2006

Distribution of extracellular matrix proteins type I collagen, type IV collagen, fibronectin, and laminin in mouse folliculogenesis.

The extracellular matrix (ECM) plays a prominent role in ovarian function by participating in processes such as cell migration, proliferation, growth, and development. Although some of these signaling processes have been characterized in the mouse, the relative quantity and distribution of ECM proteins within developing follicles of the ovary have not been characterized. This study uses immunohistochemistry and real-time PCR to characterize the ECM components type I collagen, type IV collagen, fibronectin, and laminin in the mouse ovary according to follicle stage and cellular compartment. Collagen I was present throughout the ovary, with higher concentrations in the ovarian surface epithelium and follicular compartments. Collagen IV was abundant in the theca cell compartment with low-level expression in the stroma and granulosa cells. The distribution of collagen was consistent throughout follicle maturation. Fibronectin staining in the stroma and theca cell compartment increased throughout follicle development, while staining in the granulosa cell compartment decreased. Heavy staining was also observed in the follicular fluid of antral follicles. Laminin was localized primarily to the theca cell compartment, with a defined ring at the exterior of the follicular granulosa cells marking the basement membrane. Low levels of laminin were also apparent in the stroma and granulosa cell compartment. Taken together, the ECM content of the mouse ovary changes during follicular development and reveals a distinct spatial and temporal pattern. This understanding of ECM composition and distribution can be used in the basic studies of ECM function during follicle development, and could aid in the development of in vitro systems for follicle growth.

Animals↗
PubMed1994

Relative overexpression of collagen type I and collagen type III messenger ribonucleic acids by uterine leiomyomas during the proliferative phase of the menstrual cycle.

Uterine leiomyomas contain abundant quantities of extracellular matrix (ECM). We characterized the localization of three ECM proteins, collagen type I, collagen type III, and fibronectin, in leiomyomas and adjacent normal myometrium. We further examined the expression of messenger ribonucleic acid (mRNA) levels for these proteins from 1) women who were in various stages of the menstrual cycle and 2) multiple leiomyomas from the same patient. Immunohistochemical staining showed that fibronectin was localized primarily around individual smooth muscle cells (SMC). Collagen type I was distributed across the ECM and also in the cytoplasm of SMC. Collagen type III was found primarily in the ECM. Leiomyomas showed more intense staining for collagen types I and III than corresponding normal myometrium. Northern blot and densitometric analysis showed that both collagen type I and III mRNAs were consistently elevated in leiomyomas relative to the adjacent myometrium in patients who were in the proliferative phase of the menstrual cycle (P < 0.02 for both). These differences were not evident in the secretory phase. Fibronectin mRNA levels were quite variable, and there were no significant differences between the two tissues at any stage of the menstrual cycle. We conclude that leiomyomas show increased levels of mRNA for collagen types I and III relative to the normal myometrium. However, this difference is only manifested during the proliferative phase of the menstrual cycle. These findings suggest that leiomyomas may be more sensitive to the hormonal changes that occur during the menstrual cycle than is normal myometrium.

Blotting, Northern↗
PubMedDate not supplied

Leucocyte migration inhibition with collagen type I and collagen type III in rheumatoid arthritis and degenerative joint diseases.

The leucocytes of 22 patients with classic rheumatoid arthritis were investigated with the direct leucocyte migration inhibition technique in agarose as described by Clausen. The leucocytes of 9 patients with degenerative joint diseases and of 9 healthy persons served as controls. Collagen type I and collagen type III were used as antigens. The leucocytes of 22 patients with rheumatoid arthritis showed in 15 cases a migration inhibition with collagen type III and in 10 cases with collagen type I. The inhibition with collagen type III was stronger and more frequent than with collagen type I. The frequent leucocyte migration inhibition with collagen type III in classic rheumatoid arthritis seems to be an expression of possible cell mediated reactivity against that type of collagen which appears especially in rheumatoid synovial tissue.

Adult↗
PubMed1997

Distribution of fibronectin, type I collagen, type IV collagen, and laminin in the cardiac jelly of the mouse embryonic heart with retinoic acid-induced complete transposition of the great arteries.

BACKGROUND: In the mouse model of complete transposition of the great arteries (TGA) produced by all-trans retinoic acid (RA), parietal and septal ridges in the outflow tract (OT) are hypoplastic. At first, these ridges are generated by an expanded cardiac jelly (mainly myocardial basement membrane). Thereafter, endothelial cells delaminate and invade into the adjacent cardiac jelly to form endocardial cushion tissue (formation of cushion ridge). During cushion tissue formation, basement membrane antigens play an important role in the regulation of this endothelial-mesenchymal transformation. METHODS: To examine whether the myocardial basement membrane components are altered in the RA-treated heart OT, immunohistochemistry for fibronectin, type I collagen, type IV collagen, and laminin was carried out in mouse embryonic hearts at 9.5 and 10.5 ED (embryonic day; vaginal plug = day 0) with or without prior exposure to RA. RESULTS: Particulate/fibrillar fibronectin and fibrillar type I collagen were observed in the thick cardiac jelly of the control heart at the onset of mesenchymal formation. In the RA-treated heart, an intermittent patchy staining for fibronectin and a sparse distribution of type I collagen were observed in the thin cardiac jelly. Laminin and type IV collagen were distributed continuously on the basal surface (layer adjacent to the basal plasma membrane) of endocardium and myocardium in both control and RA-treated hearts. CONCLUSIONS: The alterations in the antigens of the myocardial basement membrane (cardiac jelly) may be responsible for the hypoplasticity of parietal and septal ridges that characterizes RA-induced TGA morphology. This may be one of the reasons why mesenchymal cell formation is inhibited in the RA-induced TGA.

Animals↗
PubMedDate not supplied

Leuprolide acetate-treated leiomyomas retain their relative overexpression of collagen type I and collagen type III messenger ribonucleic acid.

OBJECTIVE: To evaluate the levels of mRNA for the extracellular matrix proteins collagen type I, collagen type III, and fibronectin in leiomyomas and myometrium obtained from women treated with GnRH-agonist (GnRH-a) and to examine steroid hormone regulation of these proteins using an in vitro explant culture system. METHODS: Northern blot analysis of mRNA was obtained from hysterectomy specimens at the time of surgery or after 48 hours of in vitro steroid treatment. A portion of the tissue was processed for RNA, and the remaining tissue was used to establish explant cultures. Extracellular matrix/alpha-tubulin ratio was computed for each band, and within each experiment the lowest ratio was standardized to a value of one densitometry unit to allow for comparison among experiments. RESULTS: There is a relative overexpression of both collagen type I and collagen type III mRNAs but not fibronectin in leiomyomas compared to myometrium from the same uteri of women treated with GnRH-a. CONCLUSION: Leiomyomas obtained from women treated with GnRH-a show an up-regulation of collagens type I and type III similar to that seen in leiomyomas obtained from women in the proliferative phase of their menstrual cycles.

Antineoplastic Agents, Hormonal↗
PubMed2001

[Dynamic changes in collagen type I and collagen type III in rabbits infected with Schistosoma japonicum and the effect of gamma-interferon].

OBJECTIVE: To observe the dynamic changes in collagen type I and collagen type III in rabbits with schistosomiasis japonica and the treatment effect of gamma-interferon on the degradation of collagens in schistosomal hepatic fibrosis. METHODS: Each rabbit was infected with 80 +/- 1 S. japonicum cercariae. Liver operations were done at different time points after infection and the liver specimens were embedded with paraffin and stained with alpha-SMA, HE and picric acid-Sirius red. The stained slides were observed under polarizing microscope and different collagen areas calculated by computer imagine analysis system. At the 16th week after infection, the infected rabbits received a single dose of praziquantel and gamma-interferon for 8 weeks. RESULTS: The area percent of collagen type I at the 28th week after infection (40.14 +/- 17.00) increased about seven fold compared with the 8th week group (5.73 +/- 3.40). The area percent of collagen type III at the 28th week after infection (6.80 +/- 5.19) increased about six fold compared with the 8th week group (1.15 +/- 1.34). The alpha-SMA positive cells also increased significantly. After gamma-interferon treatment, the area percent of collagen type I and type III decreased significantly, from 18.51 +/- 7.52 and 4.63 +/- 3.64 (before treatment) to 3.09 +/- 1.54 and 0.40 +/- 0.37 (0 and 4 weeks after treatment) (P < 0.01). However, after the withdrawl of gamma-interferon treatment, the collagen degradation was reversible. CONCLUSION: Gamma-interferon is effective in the treatment of hepatic fibrosis in rabbits infected with S. japonicum, the effect being reversible.

Animals↗