描述：
F-Spondin (floor plate and thrombospondin homology), also called Spondin-1, SPON1 or
VSGP (vascular smooth muscle growth-promoting factor), is an approximately 110 kDa
secreted glycoprotein that is a member of a subgroup of TSR (thrombospondin) molecules
that are either membrane-bound or associated with the extracellular matrix (ECM) .Human
F-Spondin is synthesized as an 807 amino acid (aa) precursor with a 779 aa mature region
that includes an Nterminal reelinlike domain, an F-Spondin (FS) domain, and six C-terminal
thrombospondin (TSP) type I repeats (13). Mature human F-Spondin shares 97%, 97%, 98%
and 99% aa sequence identity with mouse, rat, bovine and canine F-Spondin, respectively.
TSP 5 and 6 bind ECM, while TSP 14 plus the FS domain may mediate repulsive activity on
motor neurons and outgrowth promoting activity on sensory neurons during development
or after injury. Crystal structure indicates that the reelinlike domain binds heparin and may
mediate weak dimerization. Plasmin cleavage generates a diffusible 95 kDa, 656 aa F-Spondin
that lacks TSP 5 and 6, while non-plasmin cleavage between the FS segment and the first TSP
repeat generates 60 kDa and 50 kDa fragments . F-Spondin shows unusual C-mannosylation
and Ofucosylation within the TSP repeats. Mammalian cells expressing F-Spondin include
floor plate epithelium, ventral motor neurons, Schwann cells, fibroblasts, hippocampal
pyramidal cells, endothelial cells, vascular smooth muscle cells and some tumor cells.
F-Spondin can either tether cells to the ECM or interfere with integrin adhesion, thus either
blocking or allowing nerve or vascular endothelial cell migration. It binds β-amyloid fibrils and
inhibits βsecretase cleavage, thus reducing A β plaque deposition associated with Alzheimer’s
disease. F-Spondin is also reported to inhibit differentiation or migration during angiogenesis
(affecting endothelial cells) and bone development (affecting osteoclast and chondrocyte
precursors).
原厂资料：
F-Spondin (floor plate and thrombospondin homology), also called Spondin-1, SPON1 or
VSGP (vascular smooth muscle growth-promoting factor), is an approximately 110 kDa
secreted glycoprotein that is a member of a subgroup of TSR (thrombospondin) molecules
that are either membrane-bound or associated with the extracellular matrix (ECM) .Human
F-Spondin is synthesized as an 807 amino acid (aa) precursor with a 779 aa mature region
that includes an Nterminal reelinlike domain, an F-Spondin (FS) domain, and six C-terminal
thrombospondin (TSP) type I repeats (13). Mature human F-Spondin shares 97%, 97%, 98%
and 99% aa sequence identity with mouse, rat, bovine and canine F-Spondin, respectively.
TSP 5 and 6 bind ECM, while TSP 14 plus the FS domain may mediate repulsive activity on
motor neurons and outgrowth promoting activity on sensory neurons during development
or after injury. Crystal structure indicates that the reelinlike domain binds heparin and may
mediate weak dimerization. Plasmin cleavage generates a diffusible 95 kDa, 656 aa F-Spondin
that lacks TSP 5 and 6, while non-plasmin cleavage between the FS segment and the first TSP
repeat generates 60 kDa and 50 kDa fragments . F-Spondin shows unusual C-mannosylation
and Ofucosylation within the TSP repeats. Mammalian cells expressing F-Spondin include
floor plate epithelium, ventral motor neurons, Schwann cells, fibroblasts, hippocampal
pyramidal cells, endothelial cells, vascular smooth muscle cells and some tumor cells.
F-Spondin can either tether cells to the ECM or interfere with integrin adhesion, thus either
blocking or allowing nerve or vascular endothelial cell migration. It binds β-amyloid fibrils and
inhibits βsecretase cleavage, thus reducing A β plaque deposition associated with Alzheimer’s
disease. F-Spondin is also reported to inhibit differentiation or migration during angiogenesis
(affecting endothelial cells) and bone development (affecting osteoclast and chondrocyte
precursors).
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