메뉴 건너뛰기




Volumn 48, Issue 10, 2000, Pages 1291-1306

Still more complexity in mammalian basement membranes

Author keywords

Agrin; Basement membrane; Collagen XVIII; Entactin; Laminin chain; Nidogen; Proteoglycan

Indexed keywords

AGRIN; COLLAGEN TYPE 4; ENTACTIN; LAMININ; PROTEOGLYCAN; PROTEOHEPARAN SULFATE;

EID: 0033808066     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/002215540004801001     Document Type: Review
Times cited : (253)

References (162)
  • 4
    • 0002524634 scopus 로고
    • Structure and supramolecular organization of basement membranes
    • (1995) Kidney Int , vol.47 , Issue.SUPPL. 49
    • Aumailley, M.1
  • 12
  • 14
    • 0029006654 scopus 로고
    • Analysis of proteoglycan expression in developing chicken brain: Characterization of a heparan sulfate proteoglycan that interacts with the neural cell adhesion molecule
    • (1995) J Neurosci Res , vol.41 , pp. 49-64
    • Burg, M.A.1    Halfter, W.2    Cole, G.J.3
  • 19
    • 0033022469 scopus 로고    scopus 로고
    • Endostatin binds to blood vessels in situ independent of heparan sulfate and does not compete for fibroblast growth factor-2 binding
    • (1999) Am J Pathol , vol.155 , pp. 71-76
    • Chang, Z.1    Choon, A.2    Friedl, A.3
  • 23
  • 28
    • 0023434151 scopus 로고
    • Heterogenous distribution of a basement membrane heparan sulfate proteoglycan in rat tissues
    • (1987) J Cell Biol , vol.105 , pp. 1901-1916
    • Couchman, J.R.1
  • 30
    • 0029931978 scopus 로고    scopus 로고
    • Perlecan and basement membrane-chondroitin sulfate proteoglycan (bamacan) are two basement membrane chondroitin/dermatan sulfate proteoglycans in the Engelbreth-Holm-Swarm tumor matrix
    • (1996) J Biol Chem , vol.271 , pp. 9595-9602
    • Couchman, J.R.1    Kapoor, R.2    Sthanam, M.3    Wu, R.-R.4
  • 31
    • 0003027506 scopus 로고
    • Structure and biology of pericellular proteoglycans
    • Roberts DD, Mecham RR, eds. Cell Surface and Extracellular Glycoconjugates. San Diego, Academic Press
    • (1993) , pp. 33-82
    • Couchman, J.R.1    Woods, A.2
  • 37
    • 0003016233 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans in basement membranes: Perlecan, agrin, and collagen XVIII
    • Iozzo RV, ed. Proteoglycans Structure, Biology, and Molecular Interactions. New York, Marcel Dekker
    • (2000) , pp. 275-326
    • Dunlevy, J.R.1    Hassell, J.R.2
  • 46
    • 0002430174 scopus 로고
    • Interstitial basement membrane components in development
    • Yurchenco PD, Birk DE, Mecham RP, eds. Extracellular Matrix Assembly and Structure. San Diego, Academic Press
    • (1994) , pp. 441-462
    • Fitch, J.M.1    Lisenmayer, T.R.2
  • 47
    • 0000409844 scopus 로고    scopus 로고
    • Matrix proteoglycans
    • Comper WD, ed. Extracellular Matrix, Molecular Components and Interactions. Amsterdam, Harwood Academic Publishers
    • (1996) , pp. 200-229
    • Fosang, A.J.1    Hardingham, T.E.2
  • 59
    • 0025773938 scopus 로고
    • Comparison of agrin-like proteins from the extracellular matrix of chicken kidney and muscle with neural agrin, a synapse organizing molecule
    • (1991) Exp Cell Res , vol.195 , pp. 99-109
    • Godfrey, E.W.1
  • 61
    • 0032126693 scopus 로고    scopus 로고
    • Mapping of the binding of platelet-derived growth factor to distinct domains of the basement membrane proteins BM-40 and perlecan and distinction from the BM-40 collagen-binding epitope
    • (1998) Eur J Biochem , vol.255 , pp. 60-66
    • Gohring, W.1    Sasaki, T.2    Heldin, C.H.3    Timpl, R.4
  • 76
    • 0018425671 scopus 로고
    • Anionic sites in the glomerular basement membrane. In vivo and vitro localization to the laminae rarae by cationic probes
    • (1979) J Cell Biol , vol.81 , pp. 137-153
    • Kanwar, Y.S.1    Farquhar, M.G.2
  • 84
  • 93
    • 0002610135 scopus 로고    scopus 로고
    • Non-integrin laminin receptors
    • Ekblom P, Timpl R, eds. The Laminins. Amsterdam, Harwood Academic Publishers
    • (1996) , pp. 159-183
    • Mecham, R.P.1    Hinek, A.2
  • 100
    • 0034650304 scopus 로고    scopus 로고
    • Defective glomerulogenesis in the absence of laminin α5 demonstrates a developmental role for the kidney glomerular basement membrane
    • (2000) Dev Biol , vol.217 , pp. 278-289
    • Miner, J.H.1    Li, C.2
  • 112
  • 115
  • 120
    • 0025350522 scopus 로고
    • Identification and characterization of a 43 kilodalton laminin fragment from the 'A' chain (long arm) with high affinity heparin binding and mammary epithelial cell adhesion-spreading activities
    • (1990) Biochemistry , vol.29 , pp. 6768-6777
    • Rao, C.N.1    Kefalides, N.A.2
  • 121
    • 0028176183 scopus 로고
    • α1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collgen
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4234-4238
    • Rehn, M.1    Pihlajaniemi, T.2
  • 122
    • 0028964416 scopus 로고
    • Identification of three N-terminal ends of type XVIII collagen chains and tissue-specific differences in the expression of the corresponding transcripts
    • (1995) J Biol Chem , vol.270 , pp. 4705-4711
    • Rehn, M.1    Pihlajaniemi, T.2
  • 123
    • 0028174283 scopus 로고
    • Primary structure of the α1 chain of mouse type XVIII collagen, partial structure of the corresponding gene, and comparison of the α1(XVIII) chain with its homologue, the α1 (XV) collagen chain
    • (1994) J Biol Chem , vol.269 , pp. 13929-13935
    • Rehn, M.1    Hintikka, E.2    Pihlajaniemi, T.3
  • 124
    • 0029867830 scopus 로고    scopus 로고
    • Characterization of the mouse gene for the a1 chain of type XVIII collagen (Col18a1) reveals that the three variant N-terminal polypeptide forms are transcribed from two widely separated promoters
    • (1996) Genomics , vol.32 , pp. 436-446
    • Rehn, M.1    Hintikka, E.2    Pihlajaniemi, T.3
  • 144
    • 0027520442 scopus 로고
    • Cell and heparin binding in the distal long arm of laminin: Identification of active and cryptic sites with recombinant and hybrid glycoprotein
    • (1993) J Cell Biol , vol.123 , pp. 1255-1268
    • Sung, U.1    O'Rear, J.J.2    Yurchenco, P.D.3
  • 157
    • 0024564197 scopus 로고
    • Agrin-induced specializations contain cytoplasmic, membrane, and extracellular matrix-associated components of the postsynaptic apparatus
    • (1989) J Neurosci , vol.4 , pp. 2346-2349
    • Wallace, B.G.1
  • 159
    • 0029004553 scopus 로고
    • Laminin is required for heart, somatic muscles and gut development in the Drosophila embryo
    • (1995) Dev Biol , vol.169 , pp. 609-618
    • Yarnitzky, T.1    Volk, T.2
  • 162
    • 0028122383 scopus 로고
    • Amino acid determinants that drive heparan sulphate assembly in a proteoglycan
    • (1994) J Biol Chem , vol.269 , pp. 19295-19299
    • Zhang, L.1    Esko, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.