scholarly journals Intracellular protein and nucleic acid measured in eight cell types using deep-ultraviolet mass mapping

2013 ◽  
Vol 83A (6) ◽  
pp. 540-551 ◽  
Author(s):  
Man C. Cheung ◽  
Rebecca LaCroix ◽  
Brian K. McKenna ◽  
Ling Liu ◽  
James Winkelman ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Cell Types ◽  
Intracellular Protein ◽  
Deep Ultraviolet ◽  
Mass Mapping

Nucleic acid and protein mass mapping by live-cell deep-ultraviolet microscopy

2007 ◽  
Vol 4 (7) ◽  
pp. 567-569 ◽  
Author(s):  
Benjamin J Zeskind ◽  
Caroline D Jordan ◽  
Winston Timp ◽  
Linda Trapani ◽  
Guichy Waller ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Live Cell ◽  
Protein Mass ◽  
Ultraviolet Microscopy ◽  
Deep Ultraviolet ◽  
Mass Mapping

scholarly journals Deep ultraviolet mapping of intracellular protein and nucleic acid in femtograms per pixel

2011 ◽  
Vol 79A (11) ◽  
pp. 920-932 ◽  
Author(s):  
Man C. Cheung ◽  
James G. Evans ◽  
Brian McKenna ◽  
Daniel J. Ehrlich
Keyword(s):  
Nucleic Acid ◽  
Intracellular Protein ◽  
Deep Ultraviolet

scholarly journals Nucleic acid-mediated intracellular protein delivery by lipid-like nanoparticles

Biomaterials ◽  
2014 ◽  
Vol 35 (24) ◽  
pp. 6454-6461 ◽  
Author(s):  
Ahmed A. Eltoukhy ◽  
Delai Chen ◽  
Omid Veiseh ◽  
Jeisa M. Pelet ◽  
Hao Yin ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Protein Delivery ◽  
Intracellular Protein ◽  
Intracellular Protein Delivery

scholarly journals Measurement and standardization challenges for extracellular vesicle therapeutic delivery vectors

Nanomedicine ◽  
2020 ◽  
Vol 15 (22) ◽  
pp. 2149-2170
Author(s):  
Bryant C Nelson ◽  
Samantha Maragh ◽  
Ionita C Ghiran ◽  
Jennifer C Jones ◽  
Paul C DeRose ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Nucleic Acid ◽  
Lipid Bilayer ◽  
Cell Types ◽  
Extracellular Vesicle ◽  
Clinical Therapeutics ◽  
Measurement Systems ◽  
Therapeutic Delivery ◽  
Efficient Delivery ◽  
Standardized Measurement

Extracellular vesicles (EVs), such as exosomes and microvesicles, are nonreplicating lipid bilayer particles shed by most cell types which have the potential to revolutionize the development and efficient delivery of clinical therapeutics. This article provides an introduction to the landscape of EV-based vectors under development for the delivery of protein- and nucleic acid-based therapeutics. We highlight some of the most pressing measurement and standardization challenges that limit the translation of EVs to the clinic. Current challenges limiting development of EVs for drug delivery are the lack of: standardized cell-based platforms for the production of EV-based therapeutics; EV reference materials that allow researchers/manufacturers to validate EV measurements and standardized measurement systems for determining the molecular composition of EVs.

scholarly journals Control of Golgi Morphology and Function by Sed5 t-SNARE Phosphorylation

2005 ◽  
Vol 16 (10) ◽  
pp. 4918-4930 ◽  
Author(s):  
Adina Weinberger ◽  
Faustin Kamena ◽  
Rachel Kama ◽  
Anne Spang ◽  
Jeffrey E. Gerst
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Trafficking ◽  
Retrograde Transport ◽  
Cell Types ◽  
Intracellular Protein ◽  
Inhibition Of Growth ◽  
Golgi Transport ◽  
Transport Vesicles ◽  
And Function ◽  
Kinase A

Previously, we demonstrated that the phosphorylation of t-SNAREs by protein kinase A (PKA) affects their ability to participate in SNARE complexes and to confer endocytosis and exocytosis in yeast. Here, we show that the presumed phosphorylation of a conserved membrane-proximal PKA consensus site (serine-317) in the Sed5 t-SNARE regulates endoplasmic reticulum (ER)-Golgi transport, as well as Golgi morphology. Sed5 is a phosphoprotein, and both alanine and aspartate substitutions in serine-317 directly affect intracellular protein trafficking. The aspartate substitution results in elaboration of the ER, defects in Golgi-ER retrograde transport, an accumulation of small transport vesicles, and the inhibition of growth of most cell types. In contrast, the alanine substitution has no deleterious effects upon transport and growth, but results in ordering of the Golgi into a structure reminiscent of mammalian apparatus. This structure seems to require the recycling of Sed5, because it was found not to occur in sec21-2 cells that are defective in retrograde transport. Thus, a cycle of Sed5 phosphorylation and dephosphorylation is required for normal t-SNARE function and may choreograph Golgi ordering and dispersal.

scholarly journals Intracellular flow cytometry staining of antibody-secreting cells using phycoerythrin-conjugated antibodies: pitfalls and solutions

2022 ◽  
Author(s):  
Patrick Renner ◽  
Michale Crone ◽  
Matthew Kornas ◽  
KimAnh Trang Pioli ◽  
Peter Dion Pioli
Keyword(s):  
Flow Cytometry ◽  
Protein Expression ◽  
Critical Role ◽  
Cell Types ◽  
Intracellular Protein ◽  
Antibody Secreting Cell ◽  
Flow Cytometry Staining ◽  
Antibody Conjugates ◽  
Accurate Comparison ◽  
Antibody Secreting Cells

Antibody-secreting cells are terminally differentiated B cells that play a critical role in humoral immunity through immunoglobulin secretion along with possessing the potential to be long-lived. It is now appreciated that antibody-secreting cells regulate multiple aspects of biology through the secretion of various cytokines. In this regard, intracellular flow cytometry is a key tool used to assess the presence of intracellular proteins such as cytokines and transcription factors. Here, we showed that the use of phycoerythrin-containing antibody conjugates led to a false interpretation of antibody-secreting cell intracellular protein expression compared to other cell types. This was mainly due to the inappropriate retention of these antibodies specifically within antibody-secreting cells. Furthermore, we demonstrated how to reduce this retention which allowed for a more accurate comparison of intracellular protein expression between antibody-secreting cells and other cell types such as B lymphocytes. Using this methodology, our data revealed that spleen antibody-secreting cells expressed Toll-like receptor 7 as well as the pro-form of the inflammatory cytokine interleukin-1β.

SEXUAL DIMORPHISM IN INTERPHASE NUCLEI OF THE LION, FELIS LEO

1965 ◽  
Vol 43 (3) ◽  
pp. 439-445
Author(s):  
Keith L. Moore
Keyword(s):  
Sexual Dimorphism ◽  
Nucleic Acid ◽  
Sex Difference ◽  
Nuclear Membrane ◽  
Sex Chromosome ◽  
Cell Types ◽  
Interphase Nuclei ◽  
X Chromosomes ◽  
Sex Chromatin ◽  
Inner Surface

A sex difference is present in the structure of interphase nuclei of somatic cells in a variety of tissues of the lion. In the female, but not in the male, there is a special mass of chromatin, the sex chromatin, which stands out from the general particulate chromatin. In neurons the sex chromatin is usually located adjacent to the nucleolus, but in other cell types it nearly always lies against the inner surface of the nuclear membrane. The sex chromatin has the cytochemical properties of desoxypentose nucleic acid and is probably derived from heterochromatic regions of one of the X-chromosomes of the female's sex chromosome complex. A mass similar to the sex chromatin of females is rarely encountered in nuclei of males. The sexual dimorphism present in interphase nuclei of the lion is similar to that described previously in other carnivores and in primates.

scholarly journals Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase

2011 ◽  
Vol 208 (4) ◽  
pp. 643-651 ◽  
Author(s):  
Sarah E. Ewald ◽  
Alex Engel ◽  
Jiyoun Lee ◽  
Miqi Wang ◽  
Matthew Bogyo ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Cell Types ◽  
Proteolytic Processing ◽  
Toll Like Receptor ◽  
The Core ◽  
Regulatory Strategy ◽  
Mouse Macrophages ◽  
Initial Cleavage ◽  
Analogous Manner ◽  
Multistep Process

Toll-like receptor (TLR) 9 requires proteolytic processing in the endolysosome to initiate signaling in response to DNA. However, recent studies conflict as to which proteases are required for receptor cleavage. We show that TLR9 proteolysis is a multistep process. The first step removes the majority of the ectodomain and can be performed by asparagine endopeptidase (AEP) or cathepsin family members. This initial cleavage event is followed by a trimming event that is solely cathepsin mediated and required for optimal receptor signaling. This dual requirement for AEP and cathepsins is observed in all cell types that we have analyzed, including mouse macrophages and dendritic cells. In addition, we show that TLR7 and TLR3 are processed in an analogous manner. These results define the core proteolytic steps required for TLR9 function and suggest that receptor proteolysis may represent a general regulatory strategy for all TLRs involved in nucleic acid recognition.

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