Cloning and characterization of a novel animal lectin expressed in the rat sublingual gland

J Histochem Cytochem. 2005 Nov;53(11):1335-43. doi: 10.1369/jhc.5A6618.2005. Epub 2005 May 27.


We cloned a rat gene that is expressed primarily in the sublingual gland and named the predicted 503 amino-acid protein SLAMP (sublingual acinar membrane protein). SLAMP has 63% homology with human ERGIC-53-like protein, a member of the family of animal L-type lectins. Using a cDNA probe for SLAMP mRNA and rabbit antisera against SLAMP, we examined the expression and localization of SLAMP in major rat organs and tissues. With both Northern and Western blot analyses, abundant expression of SLAMP was demonstrated predominantly in the sublingual gland, with single sizes of the mRNA and protein 1.8 kb and 50 kDa, respectively, but not in other organs or tissues, including the parotid and submandibular glands. With immunohistochemistry, SLAMP was localized to the mucous acinar cells, but not to the serous demilunes or the duct system. With immunoelectron microscopy, SLAMP was localized predominantly to regions corresponding to the ER-Golgi intermediate compartment. Besides the sublingual gland, SLAMP immunoreactivity was also demonstrated in mucous cells of the minor salivary glands in oral cavity and of Brunner's glands in the duodenum. These results suggested that rat SLAMP plays a specific role in the early secretory pathway of glycoproteins in specific types of mucous cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Blotting, Western
  • Cloning, Molecular
  • Humans
  • Immunohistochemistry
  • Lectins / biosynthesis
  • Lectins / genetics*
  • Mannose-Binding Lectins / genetics
  • Membrane Glycoproteins / biosynthesis
  • Membrane Glycoproteins / genetics*
  • Membrane Proteins / genetics
  • Molecular Sequence Data
  • Organ Specificity
  • RNA, Messenger / biosynthesis
  • Rabbits
  • Rats
  • Sublingual Gland / metabolism*


  • LMAN1 protein, human
  • Lectins
  • Lman1l protein, rat
  • Mannose-Binding Lectins
  • Membrane Glycoproteins
  • Membrane Proteins
  • RNA, Messenger