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Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Major sialoglycoproteins carrying polylactosaminoglycan.
Open accessAbstract
Two major lysosomal membrane glycoproteins with apparent Mr approximately 120,000 were purified from chronic myelogenous leukemia cells. These glycoproteins are major sialoglycoproteins containing polylactosaminoglycan and represent approximately 0.1-0.2% of total cell proteins. A monoclonal antibody specific to one of the glycoproteins and polyclonal antibodies specific to the other glycoprotein were obtained. Immunoelectron microscopic examination of HeLa cells revealed that these two glycoproteins mainly reside in lysosomes and multivesicular bodies. Immunoprecipitation experiments showed that a number of different cell lines express these glycoproteins. However, the apparent molecular weights differed between cell lines; this probably represents differences in the amount of polylactosaminoglycan expressed by each cell line. As shown in the following paper (Fukuda, M., Viitala, J., Matteson, J., and Carlsson, S. R. (1988) J. Biol. Chem. 263, 18920-18928) one of the glycoproteins is very homologous to that of a mouse counterpart, m-lamp-1. The human form of this glycoprotein is therefore named human lamp-1 (h-lamp-1), while the other glycoprotein, to which the monoclonal antibody was made, is called human lamp-2 (h-lamp-2). Pulse-chase labeling experiments detected that h-lamp-1 and h-lamp-2 are produced first as precursor forms of 87.5 and 84 kDa, and treatment with endo-beta-N-acetylglucosaminidase H (endo-H) or endo-beta-N-acetylglucosaminidase F (endo-F) reduced their m…
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“Further, LAMP-1 acquired appropriate N-linked glycans3839 (Fig. 6f, Supplementary Fig. 6e).”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [38]
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Defects in lysosomal enzyme trafficking
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Metadata
- Authors
- Carlsson, S. R., Roth, J., Piller, F., & Fukuda, M.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1988-12
- Volume
- 263
- Issue
- 35
- Pages
- 18911-18919
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1525792717
- Cited by
- 345
- References
- 55
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 4 · 2023: 7 · 2022: 6 · 2021: 5 · 2020: 7 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 8 · 2013: 7 · 2012: 10
- FWCI
- 4.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 28896)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- lysosomal membrane glycoprotein, LAMP1, LAMP2, lysosomes, multivesicular bodies, sialoglycoproteins, N-glycosylation, sialic acid, monoclonal antibodies, endo-beta-N-acetylglucosaminidase H, HeLa cells
- MeSH terms
- Amino Acids, Amino Sugars, Antibodies, Monoclonal, Carbohydrates, Cell Line, Glycoside Hydrolases, Humans, Lysosomes, Membrane Glycoproteins, Molecular Weight, Polymers, Polysaccharides, Sialoglycoproteins, Leukemia, Myeloid, Acute, Antigens, CD, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Lysosomal Membrane Proteins
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