Perturbation of vesicular traffic with the carboxylic ionophore monensin

Tartakoff, Alan M.

doi:10.1016/0092-8674(83)90286-6

Cited by 858 publications

(465 citation statements)

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“…4b). This ionophore (19) has little significant effect on the expression of either membrane or intracellular H-2K. However, cells pretreated for 3 h with monensin before exposure to FITC-anti-K d at 37°C showed an intracellular compartment that can no longer be replaced by newly formed vesicles.…”

Section: The Internalization Process Is Blocked By Monensin and Is Afmentioning

confidence: 97%

Spontaneous internalization of Class I major histocompatibility complex molecules in T lymphoid cells.

Tse¹,

Pernis²

1984

The Journal of Experimental Medicine

111

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A vast portion of the immunological literature has been dedicated, in the last 15 years, to the role of the major histocompatibility complex (MHC) ~ in the immune response. There is now agreement (1, 2) that the molecules coded by the genes of the MHC are essential for cellular interactions and ultimately for self, not-self distinction, at least for what concerns the response of the T system and for the production of antibodies to T-dependent antigens.In spite of the extensive efforts and of the considerable advances in the immunogenetics and biochemistry of the MHC system, several important aspects of the immune function of this system are still unknown.We have chosen to re-examine the cytology of histocompatibility antigens, with a view to some more recently investigated aspects of cell receptor dynamics, as a contribution to the knowledge of the cellular basis of MHC function. This paper is dedicated to Class I MHC molecules and T cells. It shows that Class I MHC molecules are spontaneously internalized at a rapid rate by activated T lymphoid cells in a manner that has many similarities with the recently elucidated internalization and recycling of different receptors in nonimmunocytes (3). Materials and MethodsMice. Female BALB/c, A/J, and C3H/HeJ mice were obtained from The Jackson Laboratory, Bar Harbor, ME. C3H.OL mice were obtained from Dr. A. Augustin, Columbia University, New York and bred in our animal facilities.Cell Culture. Single cell suspensions were obtained from spleens of unprimed mice 4-8 wk of age. Erythrocytes were removed by lysis with NH4CI buffer and unfractionated splenocytes were cultured at 108 cells/ml in RPMI-1640 supplemented with 10% fetal calf serum (FCS), 100 U/ml penicillin, 100 ug/ml Fungizone, 20 mM glutamine, and 5 × 10 -s M 2-mercaptoethanol in the absence or presence of either 2 t~g/ml concanavalin A (Con A), or 20 #g/ml lipopolysaccharide (LPS), or as a 1 : 1 two-way mixed-lymphocyte reaction (MLR). All tissue culture reagents were purchased from Grand Island Biological Co.,

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Section: The Internalization Process Is Blocked By Monensin and Is Afmentioning

confidence: 97%

Spontaneous internalization of Class I major histocompatibility complex molecules in T lymphoid cells.

Tse¹,

Pernis²

1984

The Journal of Experimental Medicine

111

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“…To further defi ne the proximal compartment targeting mediated by the ABCA LLLWKN motif, transfected cells expressing wild-type EGFP/SP-C or DsRed/SP-C SPPDY → LLLWKN were treated with monensin to inhibit vesicular export from the trans-Golgi ( 36 ). As Fig.…”

Section: Discussionmentioning

confidence: 99%

A novel conserved targeting motif found in ABCA transporters mediates trafficking to early post-Golgi compartments

Beers

Hawkins

Shuman

et al. 2011

Journal of Lipid Research

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“…In order to identify the subcellular compartment in which prodomain removal occurs, ADAM28-transfected COS-7 cells were subjected to pulse-chase analysis in the presence of brefeldin A (which blocks trafficking to the Golgi from the endoplasmic reticulum [48][49][50]) or monensin (which interferes with transport to late Golgi compartments [51,52]) ( Figure 3D). Treatment with Figure 4 A catalytically inactive form of ADAM28 is not converted from the pro-form into the mature form (A) Western blot of lysates from COS-7 cells transfected with a pcDNA control, wild-type ADAM28 (WT) or ADAM28 E343A (E A).…”

Section: Adam28 Immunoblotting and Processing In The Secretory Pathwaymentioning

confidence: 99%

Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28

Howard

Maciewicz

Blobel

2000

Biochemical Journal

101

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The metalloprotease disintegrins are a family of membraneanchored glycoproteins with diverse functions in fertilization, myoblast fusion, neurogenesis and protein ectodomain shedding. Here we report a cDNA sequence, encoding a metalloprotease disintegrin, termed ADAM28 (' a disintegrin and metalloprotease 28 '), which was cloned from mouse lung. From protein sequence comparisons, ADAM28 is more closely related to snake venom metalloproteases (SVMPs) than to other ADAMs, and hence may cleave similar substrates to SVMPs, perhaps including components of the extracellular matrix. Northern blot analysis of selected mouse tissues revealed that ADAM28 is expressed highly and in alternatively spliced forms in the epididymis, suggesting a possible role in sperm maturation, and at lower levels in lung. The intracellular maturation of ADAM28 expressed in COS-7 cells resembles that of other ADAMs, in that ADAM28 is made as a precursor and processed to a mature form in a late Golgi

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Perturbation of vesicular traffic with the carboxylic ionophore monensin

Cited by 858 publications

References 0 publications

Spontaneous internalization of Class I major histocompatibility complex molecules in T lymphoid cells.

Spontaneous internalization of Class I major histocompatibility complex molecules in T lymphoid cells.

A novel conserved targeting motif found in ABCA transporters mediates trafficking to early post-Golgi compartments

Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28

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