Laminin-11

Jeffrey H. Miner, Bruce Patton

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Laminins are a family of glycoproteins which are ubiquitous components of basement membranes and play key structural and functional roles. Eleven isoforms have been identified to date; each is an αβγ heterotrimer assembled from a repertoire of five α, three β and two γ chains. Studies of laminin-11 (α5β2γ1) illustrate the unique expression patterns and distinct functions that can be displayed by laminin isoforms. Laminin-11 is found in the glomerular basement membrane in kidney, in the neuromuscular synaptic cleft in skeletal muscle and in other tissues such as placenta and lung. Mice lacking laminin-11 exhibit defective glomerular filtration and developmental defects in neuromuscular synapse formation, with Schwann cells invading the synaptic cleft. Consistent with these observations, both motoneurons and Schwann cells distinguish laminin-11 from other isoforms in vitro. These results suggest that laminin-11 is a structural component of the basement membrane which influences cell behavior in physiologically relevant ways. A greater understanding of laminin-11 assembly and basement membrane incorporation could provide a logical basis for therapy in merosin-deficient congenital muscular dystrophy. Copyright (C) 1999 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)811-816
Number of pages6
JournalInternational Journal of Biochemistry and Cell Biology
Volume31
Issue number8
DOIs
StatePublished - Aug 1999

Fingerprint

Laminin
Basement Membrane
Protein Isoforms
Schwann Cells
Cells
Glomerular Basement Membrane
Motor Neurons
Synapses
Placenta
Glycoproteins
Skeletal Muscle
Muscle
Kidney
Lung
Tissue
Defects

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Cite this

Laminin-11. / Miner, Jeffrey H.; Patton, Bruce.

In: International Journal of Biochemistry and Cell Biology, Vol. 31, No. 8, 08.1999, p. 811-816.

Research output: Contribution to journalArticle

Miner, Jeffrey H. ; Patton, Bruce. / Laminin-11. In: International Journal of Biochemistry and Cell Biology. 1999 ; Vol. 31, No. 8. pp. 811-816.
@article{7abb96aad58849acaaf5e3dca3235e67,
title = "Laminin-11",
abstract = "Laminins are a family of glycoproteins which are ubiquitous components of basement membranes and play key structural and functional roles. Eleven isoforms have been identified to date; each is an αβγ heterotrimer assembled from a repertoire of five α, three β and two γ chains. Studies of laminin-11 (α5β2γ1) illustrate the unique expression patterns and distinct functions that can be displayed by laminin isoforms. Laminin-11 is found in the glomerular basement membrane in kidney, in the neuromuscular synaptic cleft in skeletal muscle and in other tissues such as placenta and lung. Mice lacking laminin-11 exhibit defective glomerular filtration and developmental defects in neuromuscular synapse formation, with Schwann cells invading the synaptic cleft. Consistent with these observations, both motoneurons and Schwann cells distinguish laminin-11 from other isoforms in vitro. These results suggest that laminin-11 is a structural component of the basement membrane which influences cell behavior in physiologically relevant ways. A greater understanding of laminin-11 assembly and basement membrane incorporation could provide a logical basis for therapy in merosin-deficient congenital muscular dystrophy. Copyright (C) 1999 Elsevier Science Ltd.",
author = "Miner, {Jeffrey H.} and Bruce Patton",
year = "1999",
month = "8",
doi = "10.1016/S1357-2725(99)00030-8",
language = "English (US)",
volume = "31",
pages = "811--816",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
publisher = "Elsevier Limited",
number = "8",

}

TY - JOUR

T1 - Laminin-11

AU - Miner, Jeffrey H.

AU - Patton, Bruce

PY - 1999/8

Y1 - 1999/8

N2 - Laminins are a family of glycoproteins which are ubiquitous components of basement membranes and play key structural and functional roles. Eleven isoforms have been identified to date; each is an αβγ heterotrimer assembled from a repertoire of five α, three β and two γ chains. Studies of laminin-11 (α5β2γ1) illustrate the unique expression patterns and distinct functions that can be displayed by laminin isoforms. Laminin-11 is found in the glomerular basement membrane in kidney, in the neuromuscular synaptic cleft in skeletal muscle and in other tissues such as placenta and lung. Mice lacking laminin-11 exhibit defective glomerular filtration and developmental defects in neuromuscular synapse formation, with Schwann cells invading the synaptic cleft. Consistent with these observations, both motoneurons and Schwann cells distinguish laminin-11 from other isoforms in vitro. These results suggest that laminin-11 is a structural component of the basement membrane which influences cell behavior in physiologically relevant ways. A greater understanding of laminin-11 assembly and basement membrane incorporation could provide a logical basis for therapy in merosin-deficient congenital muscular dystrophy. Copyright (C) 1999 Elsevier Science Ltd.

AB - Laminins are a family of glycoproteins which are ubiquitous components of basement membranes and play key structural and functional roles. Eleven isoforms have been identified to date; each is an αβγ heterotrimer assembled from a repertoire of five α, three β and two γ chains. Studies of laminin-11 (α5β2γ1) illustrate the unique expression patterns and distinct functions that can be displayed by laminin isoforms. Laminin-11 is found in the glomerular basement membrane in kidney, in the neuromuscular synaptic cleft in skeletal muscle and in other tissues such as placenta and lung. Mice lacking laminin-11 exhibit defective glomerular filtration and developmental defects in neuromuscular synapse formation, with Schwann cells invading the synaptic cleft. Consistent with these observations, both motoneurons and Schwann cells distinguish laminin-11 from other isoforms in vitro. These results suggest that laminin-11 is a structural component of the basement membrane which influences cell behavior in physiologically relevant ways. A greater understanding of laminin-11 assembly and basement membrane incorporation could provide a logical basis for therapy in merosin-deficient congenital muscular dystrophy. Copyright (C) 1999 Elsevier Science Ltd.

UR - http://www.scopus.com/inward/record.url?scp=0032867072&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032867072&partnerID=8YFLogxK

U2 - 10.1016/S1357-2725(99)00030-8

DO - 10.1016/S1357-2725(99)00030-8

M3 - Article

VL - 31

SP - 811

EP - 816

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

IS - 8

ER -