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Knockdown of Lama4 in zebrafish resulted inthe same kind of cardiac dysfunction & hemorrhages seen in Ilk mutants. There is epistatic regulation between laminin-alpha4 (Lama4), integrin, and Ilk.
Disruption of LAMA4, LAMA5 (show LAMA5 Proteins), and LAMB2 (show LAMB2 Proteins) or the laminin-receptor interaction occurs in neuromuscular diseases including Pierson syndrome and Lambert-Eaton myasthenic syndrome (LEMS). (Review)
highlight MCAM (show MCAM Proteins) and LAMA4 as prime candidates for RCC (show XRCC1 Proteins) prognosis and therapeutic targeting
LAMA4-integrin signalling affects chondrocyte morphology and gene expression, contributing to cluster formation in osteoarthritic chondrocytes.
LAMA4 expression is lowered in preeclamptic placentas and promotes trophoblast cell invasion, migration, and angiogenesis. hypoxia-reoxygenation decreases LAMA4 expression and decouple the relationship between LAMA4 expression and p38 (show CRK Proteins) and ERK (show EPHB2 Proteins) activation.
Oxidative stress plays a vital role in controlling expression of LAMA4 through MAPK (show MAPK1 Proteins) signaling pathways, which suggests a possible pathological mechanism of pre-eclampsia.
Laminins 411 and 421 differentially promote tumor cell migration via alpha6beta1 integrin and MCAM (CD146 (show MCAM Proteins)).
These results indicate that mAbs to the laminin a4 globular domain are able to inhibit tumor cell adhesion and migration on laminins 411 and 421, and that alpha6beta1 integrin and MCAM (show MCAM Proteins) bind a4-laminins at very close sites on the globular domain
laminin alpha4 LG4 module may play an important role in cell adhesion and/or vessel wall formation in the skin by interacting with syndecan-2 (show SDC2 Proteins) and/or -4.
alpha4 chain Lms have a de-adhesive function and could thus play a role in detachment, migration and invasion of renal carcinoma cells in vivo.
2 novel mutations (2828C>T [Pro943Leu] & 3217C>T [Arg1073X]) in the integrin-interacting domain of the LAMA4 gene reduce its integrin binding, & cause endothelial cell loss and heart failure.
Data (including data from studies in knockout mice) suggest that Lama4 is involved in regulation of energy metabolism, regulation of adiposity, and development of beige adipose tissue; here, Lama4 knockout mice exhibit significantly improved insulin (show INS Proteins) sensitivity compared with wild-type mice, suggesting improved metabolic function.
Results showed maintained perturbed transmission properties at lama4(-/-) NMJs from adult (3 months) through to aged (18-22 months). Hind-limb grip force demonstrated similar trends as transmission properties, with maintained weaker grip force across age groups in lama4(-/-). Interestingly, both transmission properties and hind-limb grip force in aged wild-types resembled those observed in adult lama4(-/-).
Lama4-/- NMJs demonstrated a decrease in miniature end-plate potential (EPP (show EPX Proteins)) frequency and increased amplitude of miniature EPPs and evoked EPPs.
Failure of laminin alpha4-mediated down-regulation of PDGF (show PDGFA Proteins) activity contributes to the progressive renal lesions in this animal model.
biological functions of the laminin alpha 4 chain G domain and screening of active sites
The activity of a cyclic peptide from a region of laminin alpha 4 on the connecting loop between the E and F strands is highly conformation-dependent, suggesting that the E-F loop structure is crucial for its biological activity.
These results suggest that the cryptic alpha4 LG4-5 fragment derived from the laminin alpha4 chain inhibits de novo adipogenesis by modulating the effect of FGF-2 (show FGF2 Proteins) through syndecans.
Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the alpha chain isoform laminin, alpha 4. The domain structure of alpha 4 is similar to that of alpha 3, both of which resemble truncated versions of alpha 1 and alpha 2, in that approximately 1,200 residues at the N-terminus (domains IV, V and VI) have been lost. Laminin, alpha 4 contains the C-terminal G domain which distinguishes all alpha chains from the beta and gamma chains. The RNA analysis from adult and fetal tissues revealed developmental regulation of expression, however, the exact function of laminin, alpha 4 is not known. Tissue-specific utilization of alternative polyA-signal has been described in literature. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
laminin, alpha 4
, laminin subunit alpha-4
, laminin subunit alpha-4-like
, laminin alpha 4 chain
, laminin [a]4
, laminin-14 subunit alpha
, laminin-8 subunit alpha
, laminin-9 subunit alpha