Collagen and related research最新文献_第3页

Monoclonal Antibodies for the Different Chains of Chick Type VI Collagen 鸡VI型胶原蛋白不同链的单克隆抗体

Collagen and related research Pub Date : 1988-07-01 DOI: 10.1016/S0174-173X(88)80004-9

Alfonso Colombatti , Kevin Ainger , Maria Teresa Mucignat , Paolo Bonaldo

引用次数: 8

Lysyl Oxidase in Osteogenesis Imperfecta and Marfan's Syndrome 赖氨酸氧化酶与成骨不全和马凡氏综合征的关系

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80028-1

Peter M. Royce , Beat Steinmann

引用次数: 2

Collagen Organisation in the Cervix and its Relation to Mechanical Function 子宫颈胶原组织及其与力学功能的关系

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80022-0

Richard M. Aspden

引用次数: 133

Fifth Annual Symposium of the Skin Pharmacology Society, Hotel Lutetia, Paris, France 第五届皮肤药理学学会年会，法国巴黎，Lutetia酒店

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80029-3

引用次数: 0

Interaction of Type I Collagen with Phosphatidylcholine Vesicles I型胶原蛋白与磷脂酰胆碱囊泡的相互作用

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80025-6

Alvaro Martinez del Pozo , Mercedes Oñaderra , José Laynez , José G.^Gavilanes

引用次数: 11

1st International Congress on Mucopolysaccharidosis and Related Diseases, Radisson University Hotel, Minneapolis, USA 第一届粘多糖病及相关疾病国际会议，美国明尼阿波利斯市丽笙大学酒店

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80030-X

引用次数: 0

Type IV Collagen and Laminin in Slow and Fast Skeletal Muscle in Rats — Effects of Age and Life-Time Endurance Training 大鼠慢速和快速骨骼肌中的IV型胶原蛋白和层粘连蛋白-年龄和终生耐力训练的影响

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80026-8

Vuokko Kovanen , Harri Suominen , Juha Risteli , Leila Risteli

{"title":"Type IV Collagen and Laminin in Slow and Fast Skeletal Muscle in Rats — Effects of Age and Life-Time Endurance Training","authors":"Vuokko Kovanen , Harri Suominen , Juha Risteli , Leila Risteli","doi":"10.1016/S0174-173X(88)80026-8","DOIUrl":"10.1016/S0174-173X(88)80026-8","url":null,"abstract":"<div><p>The changes in the biochemical composition of basement membrane (BM) inslowtwitch (m. soleus, MS) and fast-twitch (m. rectus femoris, MRF) skeletal muscles of rats were studied during aging and life-time endurance training (treadmill running). The concentrations of the 7S domain of type IV collagen and of the P2 fragment of laminin were determined with radioimmunoassays in the muscles of rats aged 1, 2, 4, 10, and 24 months. The concentration of type IV collagen was higher in MS than in MRF and increased significantly with age. At older ages, the concentration tended to be higher in the MS of trained than untrained rats. The concentration of laminin was significantly higher in MRF than in MS, especially in old age. Consequently, the ratio of type IV collagen to laminin was significantly higher in MS than in MRF, the difference increasing with advancing age. The results show that the Ws in slow muscle are much more collagenous than those in fast muscle which contains, on the contrary, a higher concentration of laminin. This difference seems only partly to be explained by the higher capillarization of slow twitch muscle fibers. Aging and training seem further to distinguish the composition of the BM in slow and fast muscle.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"8 2","pages":"Pages 145-153"},"PeriodicalIF":0.0,"publicationDate":"1988-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(88)80026-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14503034","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 64

Gelatinase Contributes to the Degradation of Glomerular Basement Membrane Collagen by Human Neutrophils 明胶酶参与人中性粒细胞对肾小球基底膜胶原蛋白的降解

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80023-2

Margret C.M. Vissers , Christine C. Winterbourn

{"title":"Gelatinase Contributes to the Degradation of Glomerular Basement Membrane Collagen by Human Neutrophils","authors":"Margret C.M. Vissers , Christine C. Winterbourn","doi":"10.1016/S0174-173X(88)80023-2","DOIUrl":"10.1016/S0174-173X(88)80023-2","url":null,"abstract":"<div><p>Neutrophils contain a number of proteinases active at neutral pH which are able todegrade extracellular matrices. We have determined the contribution of the major neutral proteinases to human neutrophil-mediated degradation of glomerular basement membrane type IV collagen in an <em>in vitro</em> model of immune complex-induced injury. Studies with proteinase inhibitors showed that with intact neutrophils stimulated by immune complexes trapped within the basement membrane, approximately 70% of the degradation was due to serine proteinases and 30% to metalloproteinases. Identical results were obtained with cell-free medium containing neutrophil granule contents. Elastase accounted for almost all the digestion by serine proteinases with a minimal contribution by cathepsin G. All the metalloproteinase activity was due to gelatinase rather than collagenase, and purified gelatinase was also shown to degrade basement membrane collagen. Hence, gelatinase has activity against type IV collagen and may be able to degrade collagens not cleaved by specific collagenases.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"8 2","pages":"Pages 113-122"},"PeriodicalIF":0.0,"publicationDate":"1988-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(88)80023-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13974307","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 32

Schwann Cells and Collagen Synthesis in Taxol-Treated Nerve Crush. An Electron Microscopic Study 许旺细胞和胶原合成在紫杉醇治疗的神经压迫。电子显微镜研究

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80024-4

Matias Röyttä , Juha Peltonen , Ville Vuorinen

{"title":"Schwann Cells and Collagen Synthesis in Taxol-Treated Nerve Crush. An Electron Microscopic Study","authors":"Matias Röyttä , Juha Peltonen , Ville Vuorinen","doi":"10.1016/S0174-173X(88)80024-4","DOIUrl":"10.1016/S0174-173X(88)80024-4","url":null,"abstract":"<div><p>The effect of nerve crush on collagen synthesis in rat sciatic nerve was studied byelectron microscope. The crushed nerves were treated with taxol which is known to increase the amount of cytoplasmic microtubules at the expense of other cell organelles such as rough endoplasmic reticulum and Golgi complexes. The results were compared to those seen in crushed nerves without taxol treatment.</p><p>After the injury the amount of collagen fibrils increased at the site of the traumain both groups when compared to intact controls. Thin (30 mn in diameter) collagen firils were often arranged closely to the Schwann cell surface and were connected to deep invaginations in areas where the basal lamina had lost its typical integrity. This was concluded to indicate a probable site of collagen secretion and it provides further evidence that an adult injured nerve Schwann cell is capable of synthesizing fibrous collagen.</p><p>In taxol-treated nerves additional, abnormally close connection between thinmicrofibrils of about 10 nm and thin 20-30 nm collagen fibrils appeared in an end-to-end fashion. The microfibrils showed occasional collagenous transverse band like structures. The rough endoplasmic reticulum and Golgi complex play an important role in the posttranslational modifications of the procollagen molecule. Taxol-induced degeneration of cell organelles such as the Golgi complex, which is also essential in the secretion of proteins may thus lead to defective maturation of collagen and may explain partly the altered collagen fibril formation.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"8 2","pages":"Pages 123-131"},"PeriodicalIF":0.0,"publicationDate":"1988-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(88)80024-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14034081","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

Focal Adhesions and Cell-Matrix Interactions 病灶黏附和细胞-基质相互作用

Collagen and related research Pub Date : 1988-03-01 DOI: 10.1016/S0174-173X(88)80027-X

Anne Woods , John R. Couchman

引用次数: 96