Differential Expression of the Lysosome-Associated Membrane Proteins in Normal Human Tissues

Furuta, Koh; Yang, Xiao; Chen, Juei Suei; Hamilton, Stanley R.; August, J. Thomas

doi:10.1006/abbi.1999.1147

Cited by 52 publications

(46 citation statements)

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“…19 Although previous immunohistochemical and electron microscopic studies 9 uniformly support the conclusion that LAMP molecules have a predominant steady-state localization in the lysosome, we showed that some human tissue cells have dissociation between expression of LAMP proteins and lysosomal hydrolases. 19 Moreover, the azurophilic granules that are defined as primary lysosomes, ie, a membrane-bound organelle containing acid hydrolases, in neutrophilic leukocytes and their precursors in the bone marrow have little of the LAMP molecules. 22 It has been observed repeatedly that neoplastic transformation is associated with a variety of structural changes in cell surface carbohydrates, most notably increased sialylation and ␤1-6-linked branching of complex-type asparagine (Asn)-linked oligosaccharides (-GlcNAc␤1-6Man␣1-6Man␤1-).…”

mentioning

confidence: 44%

“…9,11-15 LAMP-2 is also found as splice variant molecules that are encoded by at least two or three transcripts resulting in variant transmembrane and cytoplasmic domains. Three transcripts in chicken 16 and mouse 16,17 and two human transcripts 18,19 have been reported to date. Although the LAMP proteins have assumed importance as markers of lysosomes in a wide variety of biological studies, the function of the molecules is not proved.…”

mentioning

confidence: 99%

“…One speculation is that LAMP-1 is a housekeeping protein 20,21 whereas LAMP-2 may have some additional or other role. 19 In a previous study, we conducted an immunohistochemical and molecular analysis of the relative degree of expression of LAMP-1 as compared to LAMP-2 in various normal human tissues. 19 Although previous immunohistochemical and electron microscopic studies 9 uniformly support the conclusion that LAMP molecules have a predominant steady-state localization in the lysosome, we showed that some human tissue cells have dissociation between expression of LAMP proteins and lysosomal hydrolases.…”

mentioning

confidence: 99%

“…19 In a previous study, we conducted an immunohistochemical and molecular analysis of the relative degree of expression of LAMP-1 as compared to LAMP-2 in various normal human tissues. 19 Although previous immunohistochemical and electron microscopic studies 9 uniformly support the conclusion that LAMP molecules have a predominant steady-state localization in the lysosome, we showed that some human tissue cells have dissociation between expression of LAMP proteins and lysosomal hydrolases. 19 Moreover, the azurophilic granules that are defined as primary lysosomes, ie, a membrane-bound organelle containing acid hydrolases, in neutrophilic leukocytes and their precursors in the bone marrow have little of the LAMP molecules.…”

mentioning

confidence: 99%

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Expression of Lysosome-Associated Membrane Proteins in Human Colorectal Neoplasms and Inflammatory Diseases

Furuta

Ikeda

Nakayama

et al. 2001

The American Journal of Pathology

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The lysosome-associated membrane proteins (LAMPs)-1 and -2 are major constituents of the lysosomal membrane. These molecules are known to be among the most glycosylated proteins of several types of cells and cancer cells, and their expression in cancer cells is marked by a distinct difference in the structures of the oligosaccharides as compared to nonmalignant cells. We analyzed by immunohistochemistry the intensity and distribution of LAMP-1 and LAMP-2 in 9 human colorectal cancer cases and in 16 control cases, including inflammatory diseases (diverticulitis, ulcerative colitis, and Crohn's disease). LAMP proteins were expressed more intensely in the epithelium of colorectal neoplasms than in normal mucosa (P < 0.05), and no significant differences were found between adenoma and cancer cells (P > 0.05) in the same tissue section.

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confidence: 44%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Expression of Lysosome-Associated Membrane Proteins in Human Colorectal Neoplasms and Inflammatory Diseases

Furuta

Ikeda

Nakayama

et al. 2001

The American Journal of Pathology

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“…The documented accumulation of acidic intracellular compartments is supportive of an affiliation with the media pH shift, by either contributing directly to the environmental acidification, or rather resulting from it, as seen in breast cancer cells (Glunde et al, 2003). Initially, we believed the upregulation of acidic vesicles reflected an increase in lysosome organelles, yet the LAMP-2 protein, expressed on lysosomal membranes in prostate tissue, decreased in expression ( Figure 4C) (Furuta et al, 1999). It was also possible that the acidic vesicles were early endosomes, yet the protein expression of early endosome marker EEA-1 was likewise reduced (Eskelinen et al, 2003).…”

Section: Accumulation Of Acidic Intracellular Vesiclesmentioning

confidence: 80%

Cellular changes in boric acid-treated DU-145 prostate cancer cells

Barranco

Eckhert

2006

Br J Cancer

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Epidemiological, animal, and cell culture studies have identified boron as a chemopreventative agent in prostate cancer. The present objective was to identify boron-induced changes in the DU-145 human prostate cancer cell line. We show that prolonged exposure to pharmacologically-relevant levels of boric acid, the naturally occurring form of boron circulating in human plasma, induces the following morphological changes in cells: increases in granularity and intracellular vesicle content, enhanced cell spreading and decreased cell volume. Documented increases in b-galactosidase activity suggest that boric acid induces conversion to a senescentlike cellular phenotype. Boric acid also causes a dose-dependent reduction in cyclins A -E, as well as MAPK proteins, suggesting their contribution to proliferative inhibition. Furthermore, treated cells display reduced adhesion, migration and invasion potential, along with F-actin changes indicative of reduced metastatic potential. Finally, the observation of media acidosis in treated cells correlated with an accumulation of lysosome-associated membrane protein type 2 (LAMP-2)-negative acidic compartments. The challenge of future studies will be to identify the underlying mechanism responsible for the observed cellular responses to this natural blood constituent.

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Influences of the lysosomal associated membrane proteins (Lamp‐1, Lamp‐2) and Mac‐2 binding protein (Mac‐2‐BP) on the prognosis of pancreatic carcinoma

Künzli

Berberat

Zhu

et al. 2001

Cancer

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BACKGROUND Lamps and Mac‐2‐BP are ligands of galectin‐3, and they were suggested to influence tumor proliferation and metastasis formation. The authors studied the expression of Lamp‐1, Lamp‐2, and Mac‐2‐BP in pancreatic carcinoma and evaluated their influence on patient prognosis. METHODS Northern blot analysis, in situ hybridization, and immunohistochemistry were performed in 12 normal and 28 pancreatic carcinoma tissue samples and in pancreatic carcinoma cell lines. The molecular findings in the tumor samples were correlated with the prognosis and histopathologic tumor characteristics. In addition, in Lamp‐1 transfected CAPAN‐1 pancreatic carcinoma cells, cell proliferation was analyzed. RESULTS Lamp‐1, Lamp‐2, and Mac‐2‐BP were overexpressed in 61% (1.6‐fold increase, not significant), 71% (3.0‐fold increase, P < 0.01), and 93% (5.6‐fold increase, P < 0.01) of the pancreatic carcinoma samples. Lamp‐1 and Lamp‐2 immunoreactivity was present at the luminal side of the ductal carcinoma cells whereas Mac‐2‐BP immunoreactivity was diffusely spread over the whole cytoplasm and the nucleolus of ductal carcinoma cells. Correlation of the molecular data with clinical patient parameters revealed that patients whose tumors exhibited high Lamp‐1 mRNA expression lived significantly longer (median, 17 months) after tumor resection than patients whose tumors exhibited low to moderate Lamp‐1 mRNA levels (median, 8 months; P < 0.02). No relation between Lamp‐2 and Mac‐2‐BP mRNA expression and any of the histopathologic parameters was found. Lamp‐1 transfected CAPAN‐1 cells showed decreased cell growth compared with the nontransfected cells. CONCLUSIONS Lamp‐1 might influence local tumor progression rather than the formation of tumor metastasis in pancreatic carcinoma, whereas Mac‐2‐BP and Lamp‐2 seem to have little influence on these parameters in pancreatic carcinoma. Cancer 2002;94:228–39. © 2002 American Cancer Society.

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Differential Expression of the Lysosome-Associated Membrane Proteins in Normal Human Tissues

Cited by 52 publications

References 40 publications

Expression of Lysosome-Associated Membrane Proteins in Human Colorectal Neoplasms and Inflammatory Diseases

Expression of Lysosome-Associated Membrane Proteins in Human Colorectal Neoplasms and Inflammatory Diseases

Cellular changes in boric acid-treated DU-145 prostate cancer cells

Influences of the lysosomal associated membrane proteins (Lamp‐1, Lamp‐2) and Mac‐2 binding protein (Mac‐2‐BP) on the prognosis of pancreatic carcinoma

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