Category: Bad Medicine
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Scalarin carries and stabilizes carotenoid pigments
Scalarin (PsSC) is the most abundant perivitellin of the perivitelline fluid from Pomacea scalaris eggs. This glyco-lipo-caroteno protein is an approx. 380 kDa multimer combining multiple copies of six different 24-35 kDa subunits. As part of the petivitelline fluid, PsSC is probably playing a role as a nutrient source for the developing embryo in Pomacea scalaris eggs. As its orthologous ovorubin and PmPV1, this protein carries and stabilizes carotenoid pigments. As…
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Clusterin (apolipoprotein J)
Clusterin (apolipoprotein J) is a 75-80 kDa disulfide-linked heterodimeric protein associated with the clearance of cellular debris and apoptosis. In humans, clusterin is encoded by the CLU gene on chromosome 8. CLU is a molecular chaperone responsible for aiding protein folding of secreted proteins, and its three isoforms have been differentially implicated in pro- or antiapoptotic processes. Through this function, CLU is involved in many diseases related to oxidative stress, including neurodegenerative diseases, cancers, inflammatory diseases, and aging. Structure The CLU gene contains…
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The Membrane Attack Complex/Perforin (MACPF) superfamily aka MACPF/CDC superfamily
See also: Complement membrane attack complex The Membrane Attack Complex/Perforin (MACPF) superfamily, sometimes referred to as the MACPF/CDC superfamily, is named after a domain that is common to the membrane attack complex (MAC) proteins of the complement system (C6, C7, C8α, C8β and C9) and perforin (PF). Members of this protein family are pore-forming toxins (PFTs). In eukaryotes, MACPF proteins play a role in immunity and development. Archetypal members of the family…
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The membrane attack complex (MAC) or terminal complement complex (TCC) is a complex of proteins typically formed on the surface of pathogen cell membranes as a result of the activation of the host’s complement system, and as such is an effector of the immune system
From Wikipedia, the free encyclopedia See also: MACPF The membrane attack complex (MAC) or terminal complement complex (TCC) is a complex of proteins typically formed on the surface of pathogen cell membranes as a result of the activation of the host’s complement system, and as such is an effector of the immune system. Antibody-mediated complement activation leads to MAC deposition on the surface of infected cells. Assembly…
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Complement control protein are proteins that interact with components of the complement system
The complement system is tightly regulated by a network of proteins known as “regulators of complement activation (RCA)” that help distinguish target cells as “self” or “non-self.” A subset of this family of proteins, complement control proteins (CCP), are characterized by domains of conserved repeats that direct interaction with components of the complement system. These “Sushi” domains have…
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Complement receptor type 2 (CR2)
Complement receptor type 2 (CR2), also known as complement C3d receptor, Epstein-Barr virus receptor, and CD21 (cluster of differentiation 21), is a protein that in humans is encoded by the CR2 gene. CR2 is involved in the complement system. It binds to iC3b (inactive derivative of C3b), C3dg, or C3d. B cells express CR2 receptors on their surfaces, allowing the complement system to play a role in B-cell activation…
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A complement receptor is a membrane-bound receptor belonging to the complement system, which is part of the innate immune system
Complement receptors bind effector protein fragments that are produced in response to antigen-antibody complexes or damage-associated molecules. Complement receptor activation contributes to the regulation of inflammation, leukocyte extravasation, and phagocytosis; it also contributes to the adaptive immune response. Different complement receptors can participate in either the classical complement pathway, the alternative complement pathway, or both. Expression and function White blood cells, particularly monocytes and macrophages, express complement receptors on their surface.…
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Rosetting
Erythrocyte rosetting or E-rosetting is a phenomenon seen through a microscope where red blood cells (erythrocytes) are arranged around a central cell to form a cluster that looks like a flower. The red blood cells surrounding the cell form the petal, while the central cell forms the stigma of the flower shape. This formation occurs due to an immunological reaction between an epitope on the central cell’s surface and…
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Complement receptor type 1 (CR1)
Complement receptor type 1 (CR1) also known as C3b/C4b receptor or CD35 (cluster of differentiation 35) is a protein that in humans is encoded by the CR1 gene. This gene is a member of the regulators of complement activation (RCA) family and is located in the ‘cluster RCA’ region of chromosome 1. The gene encodes a monomeric single-pass type I membrane glycoprotein found on erythrocytes, leukocytes, glomerular podocytes, hyalocytes, and splenic follicular dendritic…
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Three-finger proteins and three-finger toxins
Three-finger proteins or three-finger protein domains (3FP or TFPD) are a protein superfamily consisting of small, roughly 60-80 amino acid residue protein domains with a common tertiary structure: three beta strand loops extended from a hydrophobic core stabilized by disulfide bonds. The family is named for the outstretched “fingers” of the three loops. Members of the family have no enzymatic activity, but are capable of forming protein-protein interactions with high specificity and affinity. The founding members of the…
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Isoleucine, Tryptophol, Sleeping Sickness, The Disulfiram Effect and One Trick Hypnotists From Hell
Isoleucine (symbol Ile or I) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH+3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a hydrocarbon side chain with a branch (a central carbon atom bound to three other carbon atoms). It is classified as a non-polar, uncharged (at physiological pH), branched-chain, aliphatic amino acid. It…
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Albumen prints and egg whites…all the rage back in the day…and a few other things
The albumen print, also called albumen silver print, was published in January 1847 by Louis Désiré Blanquart-Evrard, and was the first commercially exploitable method of producing a photographic print on a paper base from a negative. It used the albumen found in egg whites to bind the photographic chemicals to the paper and became the dominant form of photographic positives from 1855 to the start…
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Armour & Company (bad blood featuring Factor VIII product Factorate, Revlon, Stevie Nicks’ papa, poison soap, poison baby powder, a ghost town in Missouri involving CDC, EPA and the Crisco Kid, Hexachlorophene and something called 2,3,7,8-Tetrachlorodibenzo-p-dioxin) and some other bullshit
Armour & Company was an American company and was one of the five leading firms in the meat packing industry. It was founded in Chicago, in 1867, by the Armour brothers led by Philip Danforth Armour. By 1880, the company had become Chicago’s most important business and had helped make Chicago and its Union Stock Yards the center of America’s…
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The NACHT domain consists of seven distinct conserved motifs, including the ATP/GTPase specific P-loop, the Mg2+-binding site (Walker A and B motifs, respectively) and five more specific motifs
The NACHT domain is an evolutionarily conserved protein domain. This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription. Its name reflects some of the proteins that contain it: NAIP (NLP family apoptosis inhibitor protein), CIITA (that is, C2TA or MHC class II transcription activator), HET-E (incompatibility locus protein from Podospora anserina) and TEP1 (that is, TP1 or telomerase-associated protein). The NACHT domain contains 300 to 400 amino acids. It is…
