Dipeptidylamino-tripeptidylcarboxypeptidase NEMP3 and DPP3 (DPP III) are the same protein.

Earlier it was shown that a group of extracellular low-specific metallopeptidases is present in the mammalian brain Kropotova and Mosevitsky (2016) [1]. These enzymes are weakly connected to the axonal ends of neurons. They were named Neuron bound Extracellular MetalloPeptidases (NEMP).

Design of enkephalin modifications protected from brain extracellular peptidases providing long-term analgesia.

The main obstacle to the use of many therapeutic peptides in practice is their rapid destruction by extracellular peptidases. Earlier we have found that active in the extracellular medium of mammalian brain exopeptidases are unable to break the bonds formed by β-alanine. We have designed several modified forms of opioid peptide enkephalin (Tyr-Gly-Gly-Phe-Met; Enk) with end βAla: ModEnk1 (βAla-Tyr-Gly-Gly-Phe-Met-βAla), ModEnk2 (βAla-Tyr-Gly-Gly-Phe-NH), ModEnk3 (βAla-Tyr-Gly-Phe-NH).

A Group of Weakly Bound to Neurons Extracellular Metallopeptidases (NEMPs).

We have found that isolated from mammalian brain (rat, bovine) axonal endings (synaptosomes) degrade peptides of different composition. With the use of low concentration of non ionic detergent Triton X-100 (0.05-0.

Immunoelectron microscopic study of BASP1 and MARCKS location in the early and late rat spermatids.

Immunoelectron microscopy was used to locate the proteins BASP1 and MARCKS in the post-meiotic spermatids of male rat testis. It was shown that in early spermatids, BASP1 and MARCKS accumulate in chromatoid bodies, which are characteristic organelles for these cells. During spermatogenesis, while the spermatid nucleus is still active, the chromatoid body periodically moves to the cell nucleus and absorbs the precursors of definite mRNAs and small RNAs.

Ion channel activity of brain abundant protein BASP1 in planar lipid bilayers.

BASP1 (also known as CAP-23 and NAP-22) is a brain abundant myristoylated protein localized at the inner surface of the presynaptic plasma membrane. Emerging evidence suggests that BASP1 is critically involved in various cellular processes, in particular, in the accumulation of phosphatidylinositol-4,5-diphosphate (PIP(2)) in lipid raft microdomains. We have recently shown that BASP1 forms heterogeneously-sized oligomers and higher aggregates with an outward similarity to oligomers and protofibrils of amyloid proteins.

Oligomeric structure of brain abundant proteins GAP-43 and BASP1.

Brain abundant proteins GAP-43 and BASP1 participate in the regulation of actin cytoskeleton dynamics in neuronal axon terminals. The proposed mechanism suggests that the proteins sequester phosphatidylinositol-4,5-diphosphate (PIP(2)) in the inner leaflet of the plasma membrane. We found that model anionic phospholipid membranes in the form of liposomes induce rapid oligomerization of GAP-43 and BASP1 proteins.

M-calpain-mediated cleavage of GAP-43 near Ser41 is negatively regulated by protein kinase C, calmodulin and calpain-inhibiting fragment GAP-43-3.

Neuronal protein GAP-43 performs multiple functions in axon guidance, synaptic plasticity and regulation of neuronal death and survival. However, the molecular mechanisms of its action in these processes are poorly understood. We have shown that in axon terminals GAP-43 is a substrate for calcium-activated cysteine protease m-calpain, which participates in repulsion of axonal growth cones and induction of neuronal death.

Nerve ending "signal" proteins GAP-43, MARCKS, and BASP1.

Mechanisms of growth cone pathfinding in the course of neuronal net formation as well as mechanisms of learning and memory have been under intense investigation for the past 20 years, but many aspects of these phenomena remain unresolved and even mysterious. "Signal" proteins accumulated mainly in the axon endings (growth cones and the presynaptic area of synapses) participate in the main brain processes. These proteins are similar in several essential structural and functional properties.

Natural N-terminal fragments of brain abundant myristoylated protein BASP1.

BASP1 (also known as CAP-23 and NAP-22) is a novel myristoylated calmodulin-binding protein, abundant in nerve terminals. It is considered as a signal protein participating in neurite outgrowth and synaptic plasticity. BASP1 is also present in significant amounts in kidney, testis, and lymphoid tissues.