Biological molecules can have binding elements {monophore}, identifiable by mass spectrometry.
Growth-factor-related proteins {motility factor} can aid cell migration by increasing membrane ruffling, lamellae, and pseudopodia. Autocrine motility factor (AMF), autotaxin, scatter factor or hepatocyte growth factor, TGF-a or EGF, and insulin-like growth factor (IGF) have membrane receptors and stimulate chemokinesis and chemotaxis.
Cells can make cytokines and oxidizers that cause septic shock {sepsis, cell}|. Kif1C and other proteins can sequester toxins, such as anthrax toxin, in macrophages, to prevent sepsis.
Cell-cell binding {adhesion, cell}| involves cell-membrane proteins, such as integrins, cadherins, Deleted in Colon Cancer (DCC), and CEA.
B-integrin and twenty similar proteins {integrin} are transmembrane receptors for weak-binding glycoprotein adhesion molecules, such as extracellular-matrix fibronectin, collagen, vitronectin, and laminin. Inside cells, integrins link to cytoskeleton talin, vinculin, and actin microfilaments. Alpha-integrin maintains long-term potentiation (LTP) and aids memory.
E-cadherin, P-cadherin, and N-cadherin proteins {cadherin} are calcium adhesion molecules (CAM). E-cadherin is 120 kDa, spans cell membrane, and connects with catenins that link to cytoskeleton actin. Cancer cells have low cadherin and low intercellular adhesion. Protocadherin affects brain development.
Peptides {transportan} can go through membranes, using transactivation response elements in 5' long terminal repeats.
Transportan peptides can go through membranes, using conserved regions {transactivation response element} {TAR element} in 5' long terminal repeats (LTR).
Proteins {motor protein} can use ATP to bind to, and then slide on, microtubules. All eukaryotes have motor proteins. ATPases, kinesins, and dyneins are motor proteins.
kinesin
Kinesin-related proteins have similar 340-amino-acid motor domains, with one ATP-binding site and one tubulin microtubule-binding site. Microtubule-binding sites hold onto one protein strand, while ATP-binding site transfers other protein strand forward. Most kinesins move toward fast-growing microtubule end {microtubule plus}. Some kinesins move toward other microtubule end {microtubule minus}. C-terminal motor kinesin-related proteins move toward microtubule minus. Kinesin-related KHC, Unc-104, and KRP85/95 assist membrane-bound organelle transport, as well as mitosis and meiosis spindle and chromosome movements.
dynein
Cytoplasmic dyneins move microtubules that move cilia and flagella. Motor domains have elastic parts that strain and then release.
Proteins {catenin} link to cytoskeleton actin proteins.
Proteins move microtubule one step per ATP and can perform 100 steps {processive motility}.
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Date Modified: 2022.0225