Degradation of proteoglycan aggregate by a cartilage metalloproteinase. Evidence for the involvement of stromelysin in the generation of link protein heterogeneity in situ.
about
Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sitesMatrix metalloproteinases cleave at two distinct sites on human cartilage link proteinHuman link protein gene: structure and transcription pattern in chondrocytesLink protein has greater affinity for versican than aggrecanThe expression of functional link protein in a baculovirus system: analysis of mutants lacking the A, B and B' domainsArticular cartilage and osteoarthrosis. The role of molecular markers to monitor breakdown, repair and disease.VDIPEN, a metalloproteinase-generated neoepitope, is induced and immunolocalized in articular cartilage during inflammatory arthritis.Quinolone arthropathy--acute toxicity to immature articular cartilage.Articular cartilage superficial zone collagen birefringence reduced and cartilage thickness increased before surface fibrillation in experimental osteoarthritis.Studies of the articular cartilage proteoglycan aggrecan in health and osteoarthritis. Evidence for molecular heterogeneity and extensive molecular changes in disease.Aggrecan heterogeneity in articular cartilage from patients with osteoarthritis.Matrix metalloproteinases in inflammatory bowel disease: boon or a bane?Aggrecan degradation in human cartilage. Evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints.Purification and partial characterization of a novel lectin from elder (Sambucus nigra L.) fruit.Prospects of immunotherapy for rheumatoid arthritis.Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage.Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides.Pathogenesis of degenerative joint disease in the human temporomandibular joint.Inhibition of interleukin 1 beta induced rat and human cartilage degradation in vitro by the metalloproteinase inhibitor U27391.Articular cartilage destruction in experimental inflammatory arthritis: insulin-like growth factor-1 regulation of proteoglycan metabolism in chondrocytes.An N-terminal peptide from link protein is rapidly degraded by chondrocytes, monocytes and B cells.Cartilage proteoglycan aggregate is degraded more extensively by cathepsin L than by cathepsin B.Link protein as a monitor in situ of endogenous proteolysis in adult human articular cartilage.Characterization of proteoglycan degradation by calpain.N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage.Rabbit models of arthritis: immunolocalization of matrix metalloproteinases and tissue inhibitor of metalloproteinase in synovium and cartilage.A proteolytic fragment from human link protein is taken up and processed by monocytes and B cells.Quantification of a matrix metalloproteinase-generated aggrecan G1 fragment using monospecific anti-peptide serum.Degradation of human proteoglycan aggregate induced by hydrogen peroxide. Protein fragmentation, amino acid modification and hyaluronic acid cleavage.Metalloproteinase digestion of cartilage proteoglycan. Pattern of cleavage by stromelysin and susceptibility to collagenase.Osteoarthritis: differential expression of matrix metalloproteinase-9 mRNA in nonfibrillated and fibrillated cartilage.Cellular and matrix changes before and at the time of calcification in the growth plate studied in vitro: arrest of type X collagen synthesis and net loss of collagen when calcification is initiated.Purified staphylococcal culture medium stimulates neutral metalloprotease secretion from human articular cartilage.Interleukin-1alpha induction of tensile weakening associated with collagen degradation in bovine articular cartilage.RT-PCR analysis of MMP-9 expression in human articular cartilage chondrocytes and synovial fluid cells.The effect of naproxen and interleukin-1 on proteoglycan catabolism and on neutral metalloproteinase activity in normal articular cartilage in vitro.In vivo effects of stromelysin on the composition and physical properties of rabbit articular cartilage in the presence and absence of a synthetic inhibitor.Age-related changes in hyaluronan, proteoglycan, collagen, and osteonectin synthesis by human bone cells.Link protein shows species variation in its susceptibility to proteolysis.
P2860
Q24317728-EA441C6A-E9D0-4744-818E-CF42E7F58043Q24528169-95A36C97-072B-41EC-8975-61F7B7710F13Q24528454-985E2EC5-C8E4-4F77-A08F-80EEE5955F41Q28238789-C278B298-8162-48A3-B930-0DA2B9779F57Q28645708-ED48FD97-1AA1-4F31-8CB9-8E4EB75B6EBDQ34087323-DA57939C-FC3B-4FFB-8A2D-3A74B45AC6DBQ34217504-C76BDA1E-6FF9-414C-8205-9C98B0A9466CQ35209749-D89ED7D1-2BB4-48D0-9511-79809A7C7665Q35547831-51805245-5F07-4688-951A-62F501F1B80EQ35613010-144BB43B-0BDF-4527-8B90-B29576569BF2Q35927701-77456AB0-B0BD-4F7F-B46F-DAE425EF11EAQ36700657-09C0D47E-4708-4E60-A1D1-071D60E9A04AQ37369629-B32B62D1-1FA2-4300-B1DE-817AC4931137Q38333348-3CF663FE-78EE-4F3D-B4F2-9E5ACEE39FF1Q40968027-71D94852-EC77-4A68-AF37-75FBA4984C37Q41019564-A810D7E7-98AA-467C-8D26-91603DF86EF8Q41079349-64F449EE-5BB2-48FB-B184-7D79886FCB55Q41094496-13FCA233-0D37-4FBC-8688-797DB4D26E21Q41258270-E3257821-6F86-4235-964C-378C91EF7468Q41335748-2DE49A1E-FF1D-45AB-9A09-29818C7C96B9Q41573086-E040B277-8B72-4191-95AE-E85233F8C80FQ41964012-6EDB0B7E-762B-4360-AC8A-570FF1B21EB5Q42069047-9EBC8414-09AC-416A-AA55-1B81FF8BE930Q42161514-7EF60FA0-7999-4E79-A1C2-B58D44200B58Q42682254-DAB4A4CD-00FE-4691-90FE-AEF2EF9DB0ACQ42754849-34850223-271F-4E6B-851C-3C6E2B7A9268Q42792306-C93C5E09-0615-4C03-B470-2383328C29B8Q42825978-30B0E4AE-BA91-493A-AAE3-B4DD71076BD2Q42836130-97226B74-0F48-49EE-9AF8-EAE458EBD3C6Q42862684-E638EA85-608A-49B2-ADC5-718EEB7F134AQ46075426-278B6A74-0D8E-4372-AAA2-C1481EF1F206Q46295316-048174D9-480F-41AA-A0EC-55A9FD145665Q46320302-B80FEDD9-8AAF-4B0D-BDA0-FA30C29A1C59Q46351099-E0FB81DF-C697-4E6F-93BB-1C9EEB8D5A2AQ46923611-BE798DB8-1378-44C4-BD33-4680AF67BA02Q48819481-C4295161-0137-4A88-A64E-B4F7DA7213C6Q50757148-68663B7D-7346-4C8B-99F6-5523FE2E0ADEQ52421615-DA2C82D4-AF8F-4314-B36F-7EDB5A726E72Q54262520-59FE5E11-B3DE-4089-AD32-B97C4DF0582A
P2860
Degradation of proteoglycan aggregate by a cartilage metalloproteinase. Evidence for the involvement of stromelysin in the generation of link protein heterogeneity in situ.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Degradation of proteoglycan ag ...... protein heterogeneity in situ.
@en
type
label
Degradation of proteoglycan ag ...... protein heterogeneity in situ.
@en
prefLabel
Degradation of proteoglycan ag ...... protein heterogeneity in situ.
@en
P2093
P2860
P356
P1433
P1476
Degradation of proteoglycan ag ...... protein heterogeneity in situ.
@en
P2093
P2860
P356
10.1042/BJ2590061
P407
P577
1989-04-01T00:00:00Z