Massimo Sargiacomo

ORCID: 0000-0003-4040-706X
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About
Contact & Profiles
Research Areas
  • Caveolin-1 and cellular processes
  • Erythrocyte Function and Pathophysiology
  • Extracellular vesicles in disease
  • Metabolism, Diabetes, and Cancer
  • Lipid Membrane Structure and Behavior
  • Ion Transport and Channel Regulation
  • Glycosylation and Glycoproteins Research
  • RNA Interference and Gene Delivery
  • Toxin Mechanisms and Immunotoxins
  • Signaling Pathways in Disease
  • MicroRNA in disease regulation
  • Transgenic Plants and Applications
  • HIV Research and Treatment
  • Immune Cell Function and Interaction
  • RNA Research and Splicing
  • Ion channel regulation and function
  • Liver Disease Diagnosis and Treatment
  • Cellular transport and secretion
  • Hepatitis C virus research
  • Hematopoietic Stem Cell Transplantation
  • Hepatitis B Virus Studies
  • RNA regulation and disease
  • Biotin and Related Studies
  • Pancreatic function and diabetes
  • Amoebic Infections and Treatments

Istituto Superiore di Sanità
2013-2024

Center for Global Health
2023

University of Salerno
2017

Albert Einstein College of Medicine
1998-2003

University of Bologna
2002

Palmetto Hematology Oncology
2002

National Academies of Sciences, Engineering, and Medicine
1997

University of L'Aquila
1997

National Center for Tumor Diseases
1997

Thomas Jefferson University
1996-1997

Exosomes secreted by normal and cancer cells carry deliver a variety of molecules. To date, mechanisms referring to tumor exosome trafficking, including release cell-cell transmission, have not been described. gain insight into this, exosomes purified from metastatic melanoma cell medium were labeled with lipid fluorescent probe, R18, analyzed spectrofluorometry confocal microscopy. A low pH condition is hallmark malignancy, potentially influencing uptake cells. Using different conditions as...

10.1074/jbc.m109.041152 article EN cc-by Journal of Biological Chemistry 2009-10-01

Caveolae are plasma membrane specializations that have been implicated in signal transduction. Caveolin, a 21-24-kDa integral protein, is principal structural component of caveolae membranes vivo. G protein α subunits concentrated purified preparations membranes, and caveolin interacts directly with multiple subunits, including Gs, Go, Gi2. Mutational or pharmacologic activation Gα prevents the interaction proteins, indicating inactive preferentially interact caveolin. Here, we show another...

10.1074/jbc.271.16.9690 article EN cc-by Journal of Biological Chemistry 1996-04-01

GPI-linked protein molecules become Triton-insoluble during polarized sorting to the apical cell surface of epithelial cells. These insoluble complexes, enriched in cholesterol, glycolipids, and proteins, have been isolated by flotation on sucrose density gradients are thought contain putative GPI-sorting machinery. As cellular origin molecular components this complex remain unknown, we begun characterize these low-density complexes from MDCK We find that which represent 0.4-0.8% plasma...

10.1083/jcb.122.4.789 article EN The Journal of Cell Biology 1993-08-15

Caveolae are 50-100-nm membrane microdomains that represent a subcompartment of the plasma membrane. Previous morphological studies have implicated caveolae in (a) transcytosis macromolecules (including LDL and modified LDLs) across capillary endothelial cells, (b) uptake small molecules via process termed potocytosis involving GPI-linked receptor an unknown anion transport protein, (c) interactions with actin-based cytoskeleton, (d) compartmentalization certain signaling molecules,...

10.1083/jcb.126.1.111 article EN The Journal of Cell Biology 1994-07-01

Caveolae are flask-shaped plasma membrane specializations. A 22-kDa protein, caveolin, is a principal component of caveolar membranes in vivo. As recent evidence suggests that caveolae may participate G protein-coupled signaling events, we have investigated the potential interaction caveolin with heterotrimeric proteins. Using cell fractionation techniques, found mutational or pharmacologic activation Gsα prevents its cofractionation caveolin. In second independent approach, directly...

10.1074/jbc.270.26.15693 article EN cc-by Journal of Biological Chemistry 1995-06-01

A 22-kDa protein, caveolin, is localized to the cytoplasmic surface of plasma membrane specializations called caveolae. We have proposed that caveolin may function as a scaffolding protein organize and concentrate signaling molecules within Here, we show interacts with itself form homooligomers. Electron microscopic visualization these purified homooligomers demonstrates they appear individual spherical particles. By using recombinant expression glutathione S-transferase fusion defined...

10.1073/pnas.92.20.9407 article EN Proceedings of the National Academy of Sciences 1995-09-26

Caveolae, also termed plasmalemmal vesicles, are small, flask-shaped, non-clathrin-coated invaginations of the plasma membrane. Caveolin is a principal component filaments that make up striated coat caveolae. Using caveolin as marker protein for organelle, we found adipose tissue single most abundant source caveolae identified thus far. mRNA and strongly induced during differentiation 3T3-L1 fibroblasts to adipocytes; adipogenesis there dramatic increase in complexity composition...

10.1083/jcb.127.5.1233 article EN The Journal of Cell Biology 1994-12-01

Polarized epithelial cell monolayers contain two distinct plasma membrane domains as delineated by the presence of tight junctions--i.e., an apical surface that faces external environment and a basolateral functions both in cell-cell contact cell-substrate attachment. Central to understanding polarity is question how such cell-surface specializations are generated. A different class glycoproteins has recently emerged may yield new insight into mechanism underlying biogenesis this polarity....

10.1073/pnas.85.24.9557 article EN Proceedings of the National Academy of Sciences 1988-12-01

Caveolin, an integral membrane protein, is a principal component of caveolae membranes in vivo. Two isoforms caveolin have been identified: slower migrating 24-kDa species (α-isoform) and faster 21-kDa (β-isoform). Little known about how these differ, either structurally or functionally. Here we begun to study the differences between two isoforms. Microsequencing reveals that both contain internal residues 47-77. In second independent approach, recombinantly expressed caveolin-negative cell...

10.1074/jbc.270.27.16395 article EN cc-by Journal of Biological Chemistry 1995-07-01

Methodology has been developed that enables virtually complete purification and abundant recovery of early hematopoietic progenitors from normal human adult peripheral blood. A fraction the pure is multipotent (generates mixed colonies) exhibits self-renewal capacity (gives rise to blast cell colonies). This methodology provides a fundamental tool for basic clinical studies on hematopoiesis. Optimal in vitro cloning requires not only stimulatory effect interleukin-3, granulocyte-macrophage...

10.1126/science.2218497 article EN Science 1990-09-28

Caveolins-1 and -2 are normally co-expressed, they form a hetero-oligomeric complex in many cell types. These caveolin hetero-oligomers thought to represent the assembly units that drive caveolae formation <i>in vivo</i>. However, functional significance of interaction between caveolins-1 remains unknown. Here, we show caveolin-1 co-expression is required for transport caveolin-2 from Golgi plasma membrane. We identified human erythroleukemic line, K562, expresses but fails express...

10.1074/jbc.274.36.25718 article EN cc-by Journal of Biological Chemistry 1999-09-01

Caveolin-3, the most recently recognized member of caveolin gene family, is muscle-specific and found in both cardiac skeletal muscle, as well smooth muscle cells. Several independent lines evidence indicate that caveolin-3 localized to sarcolemma, where it associates with dystrophin-glycoprotein complex. However, remains unknown which component dystrophin complex interacts caveolin-3. Here, we demonstrate directly β-dystroglycan, an integral membrane Our results co-localizes,...

10.1074/jbc.m005321200 article EN cc-by Journal of Biological Chemistry 2000-12-01

Glycosyl-phosphatidylinositol (GPI)-linked proteins are transported to the apical surface of epithelial cells where they undergo cholesterol-dependent clustering in membrane micro-invaginations, termed caveolae or plasmalemmal vesicles. However, sorting machinery responsible for this caveolar-clustering mechanism remains unknown. Using transfected MDCK as a model system, we have identified complex cell molecules (80, 50, 40, 22-24, and 14 kD) that interact pH- fashion with an recombinant...

10.1083/jcb.123.3.595 article EN The Journal of Cell Biology 1993-11-01

A large number of hDAF transgenic pigs to be used for xenotransplantation research were generated by using sperm-mediated gene transfer (SMGT). The efficiency transgenesis obtained with SMGT was much greater than any other method. In the experiments reported, up 80% had transgene integrated into genome. Most carrying transcribed it in a stable manner (64%). great majority that expressed protein (83%). transmitted progeny. Expression and found caveolae as is human cells. functional based on...

10.1073/pnas.222550299 article EN Proceedings of the National Academy of Sciences 2002-10-22

Transferrin receptor 2 (TfR2) possesses a YQRV motif similar to the YTRF of transferrin 1 (TfR1) responsible for internalization and secretion through endosomal pathway. Raft biochemical dissection showed that TfR2 is component low-density Triton-insoluble (LDTI) plasma membrane domain, able co-immunoprecipitate with caveolin-1 CD81, two structural raft proteins. In addition, subcellular fractionation experiments TfR1, which spontaneously undergoes endocytosis recycling, largely distributed...

10.1242/jcs.03228 article EN Journal of Cell Science 2006-10-18

Microenvironment cues involved in melanoma progression are largely unknown. Melanoma is highly influenced its aggressive phenotype by the changes it determinates microenvironment, such as pH decrease, turn influencing cancer cell invasiveness, and tissue remodelling through an abundant secretion of exosomes, dictating strategy to whole host. A role exosomes driving under microenvironmental acidity was never described.We studied four differently staged human lines, reflecting progression,...

10.1186/s13046-018-0915-z article EN cc-by Journal of Experimental & Clinical Cancer Research 2018-10-05

Caveolae are cholesterol/sphingolipid-rich microdomains of the plasma membrane that have been implicated in signal transduction and vesicular trafficking. Caveolins a family caveolae-associated integral proteins. Caveolin-1 -2 show widest range expression, whereas caveolin-3 expression is restricted to muscle cell types. It has previously reported little or no caveolin mRNA species detectable brain by Northern blot analyses neuroblastoma lines. However, it remains unknown whether caveolins...

10.1073/pnas.95.17.10257 article EN Proceedings of the National Academy of Sciences 1998-08-18

In this study we examined the effects of target membrane cholesterol depletion and cytoskeletal changes on human immunodeficiency virus type 1 (HIV-1) Env-mediated fusion by dye redistribution assays. We found that treatment peripheral blood lymphocytes (PBL) with methyl-beta-cyclodextrin (MbetaCD) or cytochalasin reduced their susceptibility to cells expressing HIV-1 Env utilize CXCR4 CCR5. However, osteosarcoma (HOS) high levels CD4 coreceptors these agents did not affect fusion. Removal...

10.1128/jvi.76.22.11584-11595.2002 article EN Journal of Virology 2002-10-19

We used domain-selective biotinylation/125I-streptavidin blotting (Sargiacomo, M., M. P. Lisanti, L. Graeve, A. Le Bivic, and E. Rodriguez-Boulan. 1989 J. Membr. Biol. 107:277-286), in combination with lectin precipitation, to analyze the apical basolateral glycoprotein composition of Madin-Darby canine kidney (MDCK) cells explore role glycosylation targeting membrane glycoproteins. All six lectins recognized both glycoproteins, indicating that none sugar moieties detected were...

10.1083/jcb.109.5.2117 article EN The Journal of Cell Biology 1989-11-01

Abstract Raft microdomains have been shown to play a key role in T cell activation. We found that human lymphocytes the formation of functional rafts at plasma membrane was induced by priming. In resting cells from peripheral blood Lck and raft glycosphingolipid GM1 resided intracellular membranes. activation synthesis effector showed very high levels this lipid, which became predominantly associated. TCR triggering also targeting cytosolic membrane. Thus, acquire an improved signaling...

10.1002/1521-4141(200102)31:2<345::aid-immu345>3.3.co;2-c article EN European Journal of Immunology 2001-02-01
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