Author(s): Dickinson DP, Thiesse M
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Abstract An abundant 1.05 kb human lacrimal gland mRNA has been characterized by cDNA cloning. It encodes a predicted 180 residue, 20546 Da secreted protein, with a charge of +11 at ph 7 and 24.5\% proline, designated as Basic Proline-rich Lacrimal Protein (BPLP), Southern blot analysis is consistent with a single BPLP gene. BPLP lacks any distinct repetitive structure, and is unrelated to the salivary proline-rich protein super-family. The pre-proprotein shows modest overall similarity to a superfamily comprising human PRPb, the mouse MSG proteins, and rat VCS-alpha 1, VCS-beta 1 and submandibular apomucin. BPLP also contains a domain with similarity to the Zp2 protein domain found in several otherwise unrelated proteins. Northern blot analysis indicated that the BPLP gene is also expressed at modest levels in the human submandibular gland, and in situ hybridization demonstrated expression of BPLP in the secretory endpieces of the human lacrimal gland. The BPLP cDNA clone defines a new human tear protein, and should provide a useful phenotypic marker of differentiation in in vitro studies of lacrimal gland function.
This article was published in Curr Eye Res
and referenced in Biochemistry & Analytical Biochemistry