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1.
Life Sci Alliance ; 3(4)2020 04.
Article in English | MEDLINE | ID: mdl-32098784

ABSTRACT

The scavenger receptor cysteine-rich (SRCR) family of proteins comprises more than 20 membrane-associated and secreted molecules. Characterised by the presence of one or more copies of the ∼110 amino-acid SRCR domain, this class of proteins have widespread functions as antimicrobial molecules, scavenger receptors, and signalling receptors. Despite the high level of structural conservation of SRCR domains, no unifying mechanism for ligand interaction has been described. The SRCR protein SALSA, also known as DMBT1/gp340, is a key player in mucosal immunology. Based on detailed structural data of SALSA SRCR domains 1 and 8, we here reveal a novel universal ligand-binding mechanism for SALSA ligands. The binding interface incorporates a dual cation-binding site, which is highly conserved across the SRCR superfamily. Along with the well-described cation dependency on most SRCR domain-ligand interactions, our data suggest that the binding mechanism described for the SALSA SRCR domains is applicable to all SRCR domains. We thus propose to have identified in SALSA a conserved functional mechanism for the SRCR class of proteins.


Subject(s)
Calcium-Binding Proteins/genetics , Calcium-Binding Proteins/ultrastructure , DNA-Binding Proteins/genetics , DNA-Binding Proteins/ultrastructure , Tumor Suppressor Proteins/genetics , Tumor Suppressor Proteins/ultrastructure , Amino Acid Sequence/genetics , Binding Sites/genetics , Calcium-Binding Proteins/metabolism , Cysteine/metabolism , DNA-Binding Proteins/metabolism , Humans , Ligands , Protein Binding/genetics , Protein Domains/genetics , Receptors, Cell Surface/genetics , Receptors, Cell Surface/metabolism , Receptors, Scavenger/genetics , Receptors, Scavenger/metabolism , Receptors, Scavenger/ultrastructure , Tumor Suppressor Proteins/metabolism
2.
Am J Physiol Renal Physiol ; 290(1): F148-58, 2006 Jan.
Article in English | MEDLINE | ID: mdl-16131647

ABSTRACT

The adaptation of the cortical collecting duct (CCD) to metabolic acidosis requires the polymerization and deposition in the extracellular matrix of the novel protein hensin. HCO3(-)-secreting beta-intercalated cells remove apical Cl-:HCO3(-) exchangers and may reverse functional polarity to secrete protons. Using intercalated cells in culture, we found that galectin-3 facilitated hensin polymerization, thereby causing their differentiation into the H+-secreting cell phenotype. We examined the expression of galectin-3 in the rabbit kidney and its relationship to hensin during metabolic acidosis. In control kidneys, galectin-3 was expressed in the cortical and medullary collecting ducts. In the outer cortex 26 +/- 3% of CCD cells expressed galectin-3 compared with 64 +/- 3% of the cells of the inner cortex. In the CCD, galectin-3 was rarely expressed in beta-intercalated cells, being primarily present in alpha-intercalated and principal cells. During metabolic acidosis, the intensity of cellular staining for galectin-3 increased and more cells began to express it; the percentage of CCD cells expressing galectin-3 increased from 26 +/- 3 to 66 +/- 3% in the outer cortex and from 64 +/- 3 to 78 +/- 4% in the inner cortex. This was particularly evident in beta-intercalated cells where expression was found in only 8 +/- 2% in control animals but in 75 +/- 2% during metabolic acidosis in the outer cortex and similarly for the inner cortex (26 +/- 6 to 90 +/- 7%). Importantly, both galectin-3 and hensin were found in the extracellular matrix of microdissected CCDs; and during metabolic acidosis, many more cells exhibited this extracellular colocalization. Thus galectin-3 may play several important roles in the CCD, including mediating the adaptation of beta-intercalated cells during metabolic acidosis.


Subject(s)
Acidosis/metabolism , Extracellular Matrix Proteins/metabolism , Galectin 3/metabolism , Kidney Tubules, Collecting/metabolism , Kidney/metabolism , Receptors, Scavenger/metabolism , Animals , Extracellular Matrix Proteins/ultrastructure , Galectin 3/physiology , Galectin 3/ultrastructure , Immunohistochemistry , Kidney Tubules, Collecting/cytology , Mice , Microscopy, Confocal , Rabbits , Rats , Receptors, Scavenger/ultrastructure
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