Characterization of lamprin, an unusual matrix protein from lamprey cartilage: implications for evolution, structure, and assembly of elastin and other fibrillar proteins

Lamprin, an insoluble non-collagen, non-elastin protein, is the major connective tissue component of the fibrillar extracellular matrix of lamprey annular cartilage. Here we demonstrate that the soluble monomer of lamprin is a family of highly hydrophobic, self-aggregating proteins with molecular masses of 12 and 10 kDa. Two mRNAs for soluble lamprin were identified (0.9 and 2 kilobases), differing principally in the length of their 3'-untranslated tails. Variants of soluble lamprin appear to arise both as the products of multiple genes and by alternate splicing. Although not generally homologous to any other protein, soluble lamprins contain a tandemly repeated peptide sequence (GGLGY) which is present in both silkmoth chorion proteins and spider dragline silk. Strong homologies to this repeat sequence are also present in several mammalian and avian elastins. Monoclonal antibodies to VGVAPG, a repeated sequence in human elastin, also cross-react with lamprin. We suggest that these proteins share a structural motif which promotes self-aggregation and fibril formation in proteins through interdigitation of hydrophobic side chains in beta-sheet/beta-turn structures, a motif that has been preserved in recognizable form over several hundred million years of evolution.PT: J; CR: ANDERSEN SO, 1964, BIOCHIM BIOPHYS ACTA, V93, P213 BRESSAN GM, 1986, J ULTRA MOL STRUCT R, V94, P209 BRESSAN GM, 1987, BIOCHEMISTRY-US, V26, P1497 CHOTHIA C, 1982, BIOCHEMISTRY-US, V21, P3955 DONG ZY, 1991, ARCH BIOCHEM BIOPHYS, V284, P53 DORIT RL, 1990, SCIENCE, V250, P1377 ECK MJ, 1992, J BIOL CHEM, V267, P2119 GOLDSMITH MR, 1984, ANNU REV GENET, V18, P443 GOSLINE JM, 1986, ENDEAVOUR, V10, P37 GREEN NM, 1983, EMBO J, V2, P1357 HAMODRAKAS SJ, 1982, BIOCHIM BIOPHYS ACTA, V700, P42 HAMODRAKAS SJ, 1983, INT J BIOL MACROMOL, V5, P149 HAMODRAKAS SJ, 1985, J MOL BIOL, V186, P583 HAMODRAKAS SJ, 1988, PROTEIN ENG, V2, P201 HAMODRAKAS SJ, 1989, INT J BIOL MACROMOL, V11, P307 INDIK Z, 1987, P NATL ACAD SCI USA, V84, P5680 INDIK Z, 1989, AM J MED GENET, V34, P81 JONES CW, 1979, CELL, V18, P1317 KELLY J, 1988, J BIOL CHEM, V263, P980 KIMURA S, 1982, COMP BIOCH PHYSL, V73, P335 LECANIDOU R, 1983, P NATL ACAD SCI-BIOL, V80, P1955 MARSH RE, 1955, BIOCHIM BIOPHYS ACTA, V16, P1 MECHAM RP, 1991, CELL BIOL EXTRACELLU, P70 PIERCE RA, 1990, BIOCHEMISTRY-US, V29, P9677 PONTES M, 1987, BIOCHEMISTRY-US, V26, P1611 RAJU K, 1987, J BIOL CHEM, V262, P5755 SAGE H, 1982, J INVEST DERMATOL S1, V79, S146 SAGE H, 1983, COMP BIOCHEM PHYS B, V74, P373 SAMBROOK J, 1989, MOL CLONING LABORATO, V3 TAMBURRO AM, 1990, BIOPOLYMERS, V29, P855 URRY DW, 1984, J PROTEIN CHEM, V3, P403 VONHEIJNE G, 1986, NUCLEIC ACIDS RES, V14, P4683 WANG YZ, 1989, BIOCHEMISTRY-US, V28, P9801 WRIGHT GM, 1983, AM J ANAT, V167, P59 WRIGHT GM, 1983, EXPERIENTIA, V39, P495 WRIGHT GM, 1984, CAN J ZOOL, V62, P2445 XU M, 1990, P NATL ACAD SCI USA, V87, P7120; NR: 37; TC: 38; J9: J BIOL CHEM; PG: 8; GA: KG077Source type: Electronic(1