Work

Novel Regulation of Chondroitin Sulfate Glycosaminoglycan Modification of Amyloid Precursor Protein and Its Homologue, APLP2

Year: 1995

Type: article

Abstract: Alzheimer's disease is characterized by the presence of parenchymal and cerebrovascular deposits of beta-amyloid (A beta). A beta is derived from larger amyloid precursor proteins (APP), a member of a family of related polypeptides that includes amyloid precursor-like proteins, APLP1 and APLP2. APP and APLP2 isoforms are encoded by several alternatively spliced APP and APLP2 transcripts, respectively. We previously reported that the APLP2-751 isoform is modified by the addition of chondroitin sulfate glycosaminoglycan (CS GAG) at Ser-614. In this report, we demonstrate that the APLP2-763 isoform, which contains an insertion of 12 amino acids immediately N-terminal to Ser-614, is not modified by CS GAG. Finally, we demonstrate that like APLP2-751, APP isoforms that lack sequences encoded by exon 15 (L-APP) are also modified by CS GAG, whereas APP forms containing exon 15 are not. We suggest that CS GAG modification of a subset of APP and APLP2 isoforms represents a means of generating functional diversity for these polypeptides.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.270.28.16522

Authors: Gopal Thinakaran, Hilda H. Slunt, Sangram S. Sisodia

Institutions: Johns Hopkins University, Johns Hopkins Medicine

Language: English

Topic: Alzheimer's disease research and treatments

Subfield: Physiology (medical)

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430