SCF exists as two alternatively spliced variants, a soluble form and a membrane-bound form differing in one exon (exon 6). Both isoforms are initially membrane bound with an extracellular domain, a transmembrane segment and an intracellular region. The longer isoform is rapidly cleaved to generate a 165 aa soluble protein knows as sSCF. The SCF transcript that lacks exon 6 encodes a glycoprotein that remains membrane-bound (mSCF). Both mSCF and sSCF are bioactive but different in their efficacy in c-kit activation.Proteases including matrix metalloprotease-9 (Heissig et al., 2002), Chymase-1 (Longley et al., 1997) and several members of the ADAMs family (Kawaguchi et al, 2007; Amour et al, 2002; Chesneau et al, 2003; Mohan et al, 2002; Roghani et al, 1999; Zou et al, 2004) have been suggested to have a role in the processing of sSCF.
Williams, DA, Schechter, NM, Ma, Y, Tyrrell, L, Langley, K, Lu, HS, Halaban, R, Longley, BJ
Becherer, JD, Horiuchi, K, Blobel, CP, Besmer, P, Kawaguchi, N, Toyama, Y
Rönnstrand, L
Rafii, S, Hackett, NR, Moore, MA, Hattori, K, Ferris, B, Lyden, D, Friedrich, M, Besmer, P, Werb, Z, Crystal, RG, Dias, S, Heissig, B
endopeptidase activity of Endopeptidases for SCF processing [extracellular region]
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