Olfactomedin-like 3

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Therapeutic Discovery Targeting Olfactomedin-like 3 Inhibits Tumor Growth by Impairing Angiogenesis and Pericyte Coverage

Antiangiogenic drugs have been used as anticancer agents to target tumor endothelial cells or pericytes. Because of limited efficacy of the current monotherapies, there is a strong demand for the dual targeting of endothelial cells and pericytes. Here, we identify Olfactomedin-like 3 (Olfml3) as a novel proangiogenic cue within the tumor microenvironment. Tumor-derived Olfml3 is produced by bot...

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Targeting olfactomedin-like 3 inhibits tumor growth by impairing angiogenesis and pericyte coverage.

Antiangiogenic drugs have been used as anticancer agents to target tumor endothelial cells or pericytes. Because of limited efficacy of the current monotherapies, there is a strong demand for the dual targeting of endothelial cells and pericytes. Here, we identify Olfactomedin-like 3 (Olfml3) as a novel proangiogenic cue within the tumor microenvironment. Tumor-derived Olfml3 is produced by bot...

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Olfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure*

Olfactomedin-1 (Olfm1; also known as noelin and pancortin) is a member of the olfactomedin domain-containing superfamily and a highly expressed neuronal glycoprotein important for nervous system development. It binds a number of secreted proteins and cell surface-bound receptors to induce cell signaling processes. Using a combined approach of x-ray crystallography, solution scattering, analytic...

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Diversity of olfactomedin proteins in the sea urchin.

Olfactomedin (OLF) domain proteins maintain extracellular protein-protein interactions in diverse phyla. Only one OLF family member, amassin-1, has been described from the sea urchin Strongylocentrotus purpuratus, a basal invertebrate deuterostome. Amassin-1 mediates intercellular adhesion of coelomocytes (immunocytes). Here we describe the protein structural features of four additional OLF pro...

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Olfactomedin proteins: central players in development and disease

Olfactomedin proteins are characterized by a conserved domain of \texorpdfstring~\textasciitilde250 amino acids corresponding to the olfactomedin archetype first discovered in olfactory neuroepithelium. They arose early in evolution and occur throughout the animal kingdom. In mice and humans olfactomedin proteins comprise a diverse array of glycoproteins, many of which are critical for early de...

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ژورنال

عنوان ژورنال: Chinese Medical Journal

سال: 2019

ISSN: 0366-6999

DOI: 10.1097/cm9.0000000000000309