Alpha‐2‐macroglobulin: A physiological guardian

@article{Rehman2013Alpha2macroglobulinAP,
  title={Alpha‐2‐macroglobulin: A physiological guardian},
  author={Ahmed Abdur Rehman and Haseeb Ahsan and Fahim H. Khan},
  journal={Journal of Cellular Physiology},
  year={2013},
  volume={228}
}
  • A. Rehman, H. Ahsan, Fahim H. Khan
  • Published 2013
  • Chemistry, Biology, Medicine
  • Journal of Cellular Physiology
Alpha macroglobulins are large glycoproteins which are present in the body fluids of both invertebrates and vertebrates. Alpha‐2‐macroglobulin (α2M), a key member of alpha macroglobulin superfamily, is a high‐molecular weight homotetrameric glycoprotein. α2M has many diversified and complex functions, but it is primarily known by its ability to inhibit a broad spectrum of proteases without the direct blockage of the protease active site. α2M is also known to be involved in the regulation… Expand

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TLDR
It is demonstrated that an α2M derivative is capable of regulating the response to peripheral nerve injury by a mechanism that requires low‐density lipoprotein receptor‐related protein‐1. Expand
Protease activation of alpha2-macroglobulin modulates a chaperone-like action with broad specificity.
TLDR
It is proposed that alpha2M is a newly discovered and unique member of a small group of abundant extracellular proteins with chaperone properties that patrol extrace cellular spaces for unfolded/misfolded proteins and facilitate their disposal. Expand
α-Macroglobulins Are Present in Some Gram-negative Bacteria
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TLDR
Structurally characterized ECAM is an elongated, flexible molecule with overall similarities to C3 in its inactive form; activation by methylamine, chymotrypsin, or elastase induces a conformational modification reminiscent of the one undergone by the transformation of C3 into its active form, C3b. Expand
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TLDR
A new member of the α2-macroglobulin (α2M) protease inhibitor family, A2ML1 is identified, located on chromosome 12p13.31, and may play an important role during desquamation by inhibiting extracellular proteases. Expand
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TLDR
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TLDR
Western blots of conventionally collected sera showed endogenous defensins complexed with the F-form of α2M, indicating that the generation of defensin-α2M is covalently trapped via thiol-disulfide exchange. Expand
Binding of α2-macroglobulin to GRAB (Protein G-related α2-macroglobulin-binding protein), an important virulence factor of group A streptococci, is mediated by two charged motifs in the ΔA region
TLDR
Differential contribution of the arginine residues at positions 42 and 64 to α2M-binding activity and, thus, their involvement in GRAB-induced virulence are indicated. Expand
Alpha 2-macroglobulin conformation determines binding affinity for activin A and plasma clearance of activin A/alpha 2-macroglobulin complex.
TLDR
These studies reveal that alpha 2M can maintain activin A in the circulation or rapidly target the hormone for plasma clearance depending on the conformational state of the carrier protein in vivo. Expand
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TLDR
Results suggest the possible involvement of cathepsin E in disruption of the structural and functional integrity of α2M in the endolysosome system. Expand
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