Laminin-332
Laminin-332 - Related Videos
00:55
Laminins are the Adhesive Proteins of Basal Lamina
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2023
Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains. In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
06:56
Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
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Cited by 1 •
2020
We describe three methods to generate Ln1 polymers with fractal properties that signal to cells differently compared to unpolymerized Ln1.
07:18
Identification of Skeletal Muscle Satellite Cells by Immunofluorescence with Pax7 and Laminin Antibodies
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Cited by 23 •
2018
The precise identification of satellite cells is essential for studying their functions under various physiological and pathological conditions. This article presents a protocol to identify satellite cells on adult skeletal muscle sections by immunofluorescence-based staining.
10:48
Integration Free Derivation of Human Induced Pluripotent Stem Cells Using Laminin 521 Matrix
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Cited by 8 •
2017
Robust derivation of human induced pluripotent stem (hiPS) cells was achieved by using non-integrating Sendai virus (SeV) vector mediated reprogramming of dermal fibroblasts. hiPS cell maintenance and clonal expansion was performed using xeno-free and chemically defined culture conditions with recombinant human laminin 521 (LN-521) matrix and Essential E8 (E8) Medium.
13:09
Assessment of Boron Doped Diamond Electrode Quality and Application to In Situ Modification of Local pH by Water Electrolysis
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Cited by 5 •
2016
A protocol is described for the characterization of the key electrochemical parameters of a boron doped diamond (BDD) electrode and subsequent application for in situ pH generation experiments.
FAQs
Laminin-332 interaction with integrin α6β4 helps organize hemidesmosomes, which connect epithelial cells to the extracellular matrix. This receptor-associated attachment supports stable cell positioning and tissue structure. In cancer research, disruption of this relationship is important because weakened anchorage may accompany a shift toward cell behaviors linked with migration and invasion.
Proteolytic processing can modify laminin-332’s adhesive and signaling functions rather than leaving its activity unchanged. Consequently, research must consider not only how much laminin-332 is present, but also whether it has been cleaved. These changes may help explain how tumor cells lose stable matrix attachment and acquire conditions that support invasive behavior.
Changes in laminin-332 expression or deposition may weaken the organized attachment between epithelial cells and the surrounding extracellular matrix. That loss of stable tissue support can be associated with increased cell migration and invasion. Examining these changes helps connect basement-membrane disruption with the ability of cancer cells to breach tissue boundaries.
A focused investigation can examine laminin-332 expression, extracellular deposition, and proteolytic cleavage together. Researchers can then relate these molecular features to cell migration and invasion, rather than interpreting expression alone as the complete mechanism. This approach helps distinguish changes in the protein’s abundance, location, or processing that may influence cancer-related behavior.
Potentially, patterns involving laminin-332 expression, deposition, or cleavage could contribute to biomarker development. Their value would come from linking measurable changes in the basement-membrane glycoprotein with altered adhesion, migration, or invasion. In cancer research, this perspective supports investigation of laminin-332 as an indicator of tumor-associated tissue remodeling rather than as an isolated marker.
Laminin-332 is relevant because stable epithelial attachment depends on organized interactions between the basement membrane, extracellular matrix, and cell-surface receptors. When its expression, deposition, or processing changes, attachment may weaken and migration or invasion may increase. Studying these relationships clarifies mechanisms by which cancers breach basement membranes and may guide strategies targeting tumor progression.