Characterization and expression of the laminin γ3 chain:: A novel, non-basement membrane-associated, laminin chain

被引:199
作者
Koch, M
Olson, PF
Albus, A
Jin, W
Hunter, DD
Brunken, WJ
Burgeson, RE
Champliaud, MF
机构
[1] Massachusetts Gen Hosp, Cutaneous Biol Res Ctr, Boston, MA 02129 USA
[2] Harvard Univ, Sch Med, Dept Dermatol, Boston, MA 02129 USA
[3] Tufts Univ, Dept Neurosci, Sch Med, Boston, MA 02111 USA
[4] Tufts Univ, Dept Anat & Cell Biol, Sch Med, Boston, MA 02111 USA
[5] Tufts Univ, Dept Ophthalmol, Sch Med, Boston, MA 02111 USA
关键词
laminin; testis; oviduct; lung; chromosome; 9q31-34;
D O I
10.1083/jcb.145.3.605
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Laminins are heterotrimeric molecules composed of an alpha, a beta, and a gamma chain; they have broad functional roles in development and in stabilizing epithelial structures. Here, we identified a novel laminin, composed of known alpha and beta chains but containing a novel gamma chain, gamma 3. We have cloned gene encoding this chain, LAMC3, which maps to chromosome 9 at q31-34. Protein and cDNA analyses demonstrate that gamma 3 contains all the expected domains of a gamma chain, including two consensus glycosylation sites and a putative nidogen-binding site. This suggests that gamma 3-containing laminins are likely to exist in a stable matrix. Studies of the tissue distribution of gamma 3 chain show that it is broadly expressed in: skin, heart, lung, and the reproductive tracts. In skin, gamma 3 protein is seen within the basement membrane of the dermal-epidermal junction at points of nerve penetration. The gamma 3 chain is also a prominent element of the apical surface of ciliated epithelial cells of: lung, oviduct, epididymis, ductus deferens, and seminiferous tubules. The distribution of gamma 3-containing laminins on the apical surfaces of a variety of epithelial tissues is novel and suggests that they are not found within ultrastructurally defined basement membranes. It seems likely that these apical laminins are important in the morphogenesis and structural stability of the ciliated processes of these cells.
引用
收藏
页码:605 / 617
页数:13
相关论文
共 81 条
[1]   INTERNAL AMINO-ACID SEQUENCE-ANALYSIS OF PROTEINS SEPARATED BY ONE-DIMENSIONAL OR TWO-DIMENSIONAL GEL-ELECTROPHORESIS AFTER INSITU PROTEASE DIGESTION ON NITROCELLULOSE [J].
AEBERSOLD, RH ;
LEAVITT, J ;
SAAVEDRA, RA ;
HOOD, LE ;
KENT, SBH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (20) :6970-6974
[2]   BASIC LOCAL ALIGNMENT SEARCH TOOL [J].
ALTSCHUL, SF ;
GISH, W ;
MILLER, W ;
MYERS, EW ;
LIPMAN, DJ .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410
[3]  
[Anonymous], 1988, Antibodies: A Laboratory Manual
[4]   NIDOGEN MEDIATES THE FORMATION OF TERNARY COMPLEXES OF BASEMENT-MEMBRANE COMPONENTS [J].
AUMAILLEY, M ;
BATTAGLIA, C ;
MAYER, U ;
REINHARDT, D ;
NISCHT, R ;
TIMPL, R ;
FOX, JW .
KIDNEY INTERNATIONAL, 1993, 43 (01) :7-12
[5]  
Baker SE, 1996, J CELL SCI, V109, P2509
[6]   BASEMENT-MEMBRANE HEPARAN-SULFATE PROTEOGLYCAN BINDS TO LAMININ BY ITS HEPARAN-SULFATE CHAINS AND TO NIDOGEN BY SITES IN THE PROTEIN CORE [J].
BATTAGLIA, C ;
MAYER, U ;
AUMAILLEY, M ;
TIMPL, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 208 (02) :359-366
[7]   DBEST - DATABASE FOR EXPRESSED SEQUENCE TAGS [J].
BOGUSKI, MS ;
LOWE, TMJ ;
TOLSTOSHEV, CM .
NATURE GENETICS, 1993, 4 (04) :332-333
[8]   A NEW NOMENCLATURE FOR THE LAMININS [J].
BURGESON, RE ;
CHIQUET, M ;
DEUTZMANN, R ;
EKBLOM, P ;
ENGEL, J ;
KLEINMAN, H ;
MARTIN, GR ;
MENEGUZZI, G ;
PAULSSON, M ;
SANES, J ;
TIMPL, R ;
TRYGGVASON, K ;
YAMADA, Y ;
YURCHENCO, PD .
MATRIX BIOLOGY, 1994, 14 (03) :209-211
[9]   WEIGHING NAKED PROTEINS - PRACTICAL, HIGH-ACCURACY MASS MEASUREMENT OF PEPTIDES AND PROTEINS [J].
CHAIT, BT ;
KENT, SBH .
SCIENCE, 1992, 257 (5078) :1885-1894
[10]   Laminin E8 alveolarization site: Heparin sensitivity, cell surface receptors, and role in cell spreading [J].
Chen, LL ;
Shick, V ;
Matter, ML ;
Laurie, SM ;
Ogle, RC ;
Laurie, GW .
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY, 1997, 272 (03) :L494-L503