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Höning S, Sandoval IV, von Figura K (Aug 1998). "A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3". The EMBO Journal. 17 (5): 1304–14. doi: 10.1093/emboj/17.5.1304. PMC 1170479. PMID 9482728. Lee N, Wang WC, Fukuda M (Nov 1990). "Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins". The Journal of Biological Chemistry. 265 (33): 20476–87. doi: 10.1016/S0021-9258(17)30529-X. PMID 2243101. LAMP1 and LAMP2 glycoproteins comprise 50% of all lysosomal membrane proteins, [6] and are thought to be responsible in part for maintaining lysosomal integrity, pH and catabolism. [6] [11] The expression of LAMP1 and LAMP2 glycoproteins are linked, as deficiencies in LAMP1 gene will lead to increased expression of LAMP2 glycoproteins. [11] The two are therefore thought to share similar functions in vivo. [6] However, this makes the determining the precise function of LAMP1 difficult, because while the LAMP1 deficient phenotype is little different than the wild type due to LAMP2 up regulation, [6] [11] the LAMP1/ LAMP2 double deficient phenotype leads to embryonic lethality. [11] Immunofluorescence staining of HeLa Cells with antibody to reveal lysosomal LAMP1 in red and vimentin containing intermediate filaments in green. Nuclear DNA is seen in blue. Antibodies and image courtesy EnCor Biotechnology Inc.

A lamp here, a lamp there

Significant quantities of polylactosaminoglycan and sialic acid to traverse the trans- Golgi cisternae. [10]

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