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Molecular Neurodegeneration Dec 2021Neurodegenerative disorders are a group of age-associated diseases characterized by progressive degeneration of the structure and function of the CNS. Two key... (Review)
Review
BACKGROUND
Neurodegenerative disorders are a group of age-associated diseases characterized by progressive degeneration of the structure and function of the CNS. Two key pathological features of these disorders are blood-brain barrier (BBB) breakdown and protein aggregation.
MAIN BODY
The BBB is composed of various cell types and a non-cellular component---the basal lamina (BL). Although how different cells affect the BBB is well studied, the roles of the BL in BBB maintenance and function remain largely unknown. In addition, located in the perivascular space, the BL is also speculated to regulate protein clearance via the meningeal lymphatic/glymphatic system. Recent studies from our laboratory and others have shown that the BL actively regulates BBB integrity and meningeal lymphatic/glymphatic function in both physiological and pathological conditions, suggesting that it may play an important role in the pathogenesis and/or progression of neurodegenerative disorders. In this review, we focus on changes of the BL and its major components during aging and in neurodegenerative disorders, including Alzheimer's disease (AD), Parkinson's disease (PD), and amyotrophic lateral sclerosis (ALS). First, we introduce the vascular and lymphatic systems in the CNS. Next, we discuss the BL and its major components under homeostatic conditions, and summarize their changes during aging and in AD, PD, and ALS in both rodents and humans. The functional significance of these alterations and potential therapeutic targets are also reviewed. Finally, key challenges in the field and future directions are discussed.
CONCLUSIONS
Understanding BL changes and the functional significance of these changes in neurodegenerative disorders will fill the gap of knowledge in the field. Our goal is to provide a clear and concise review of the complex relationship between the BL and neurodegenerative disorders to stimulate new hypotheses and further research in this field.
Topics: Alzheimer Disease; Basement Membrane; Blood-Brain Barrier; Glymphatic System; Humans; Neurodegenerative Diseases
PubMed: 34876200
DOI: 10.1186/s13024-021-00502-y -
Current Opinion in Cell Biology Oct 1994From studies of the 'classical' components, models for the assembly and structure of an idealized basal lamina have been developed. In particular, the evidence supports... (Review)
Review
From studies of the 'classical' components, models for the assembly and structure of an idealized basal lamina have been developed. In particular, the evidence supports the concept of enmeshed collagen and laminin polymers, in which nidogen/entactin acts as a bridge between these molecules and provides anchorage for diverse matrix components. Different basement membranes, however, possess different members of the basic basal lamina families, such as the newly described alpha 6 (IV) collagen, alpha 2 (merosin) laminin, and beta 3 laminin (in kalinin/nicein) chains. Even though these members share homologous domains and sequences, and are likely to share certain functions, they also possess unique characteristics that are expected to provide for basal lamina heterogeneity. A combination of genetic, recombinant and biochemical approaches are now being applied to elucidate the special roles of both old and new components.
Topics: Animals; Basement Membrane; Calcium-Binding Proteins; Collagen; Drosophila; Heparan Sulfate Proteoglycans; Heparitin Sulfate; Humans; Laminin; Membrane Glycoproteins; Membrane Proteins; Models, Molecular; Molecular Structure; Proteoglycans
PubMed: 7833047
DOI: 10.1016/0955-0674(94)90093-0 -
Reproductive Biomedicine Online May 2021Are there differences in the composition and structure of the basal lamina surrounding follicles in prepubertal versus adult human ovarian tissue?
RESEARCH QUESTION
Are there differences in the composition and structure of the basal lamina surrounding follicles in prepubertal versus adult human ovarian tissue?
DESIGN
Frozen-thawed human ovarian tissue from six prepubertal and seven adult patients was divided into three fragments in each case: two for non-grafted tissue evaluation and one for long-term xenografting to mice. Collagen IV and laminin expression were investigated by immunohistochemistry before and after grafting. The basal lamina was analysed by transmission electron microscopy on frozen-thawed tissue.
RESULTS
In frozen-thawed tissue, collagen IV was significantly less expressed around prepubertal follicles than around adult follicles (primordial, P = 0.02; intermediate/growing follicles, P = 0.03), while laminin was significantly more expressed (primordial, P = 0.03; intermediate, P = 0.01). Collagen IV expression was significantly higher around prepubertal primordial follicles in grafted tissue than in non-grafted tissue, reaching similar levels to those in adult tissue. Ultrastructure analysis showed the basal lamina around follicles in prepubertal frozen-thawed tissue to be rather patchy and thinner than around adult follicles (primordial/intermediate, P = 0.001; primary, P = 0.02).
CONCLUSIONS
In frozen-thawed tissue, the basal lamina around prepubertal follicles is less mature than around adult follicles, but it becomes similar in both prepubertal and adult subjects after grafting. Grafting could therefore induce maturation of the basal lamina around prepubertal follicles.
Topics: Adult; Animals; Basement Membrane; Child; Child, Preschool; Collagen Type IV; Cryopreservation; Female; Humans; Infant; Laminin; Mice, SCID; Ovary; Sexual Development; Transplantation, Heterologous; Young Adult; Mice
PubMed: 33832866
DOI: 10.1016/j.rbmo.2021.02.012 -
The Journal of Investigative Dermatology Jul 1983On histologic vertical sections of skin, the epidermis is separated from the dermis by an amorphous thin membrane, the basal lamina. Ultrastructurally, the basal lamina... (Review)
Review
On histologic vertical sections of skin, the epidermis is separated from the dermis by an amorphous thin membrane, the basal lamina. Ultrastructurally, the basal lamina is composed of four areas, including the basal-cell plasma membrane and hemidesmosomes, the lamina lucida, the lamina densa, and the sub-lamina densa fibrillar region. In culture, epidermal keratinocytes are able to produce hemidesmosomes, lamina lucida, and lamina densa. There is no evidence that cultured keratinocytes can produce sub-lamina densa fibrils. Biochemically, the lamina lucida contains two major glycoproteins. One, the bullous pemphigoid antigen, is synthesized by epidermal keratinocytes in vitro. These cells also synthesize laminin, the other glycoprotein of lamina lucida. At the interface between lamina lucida and lamina densa there is probably a heparan sulfate proteoglycan. Whether this proteoglycan is produced by keratinocytes in culture is not known, but the possibility can be considered. Lamina densa contains collagen IV, and this collagen is synthesized by keratinocytes in culture. However, cultured keratinocytes may also synthesize collagen types I, III, and V. Type V is associated with the basal lamina, but its exact location is unknown. Types I and III (if they are produced in vivo) would be situated in the sub-basal lamina region. The problem of fibronectin remains unsolved. There is "some" fibronectin in the lamina lucida, but its origin is not clear.
Topics: Animals; Basement Membrane; Epidermal Cells; Fibronectins; Glycoproteins; Heparitin Sulfate; Keratins; Laminin; Microscopy, Electron; Pemphigoid, Bullous; Protein Biosynthesis; Swine
PubMed: 6190963
DOI: 10.1111/1523-1747.ep12540736 -
Current Opinion in Neurobiology Oct 2006Schwann cells form myelin in the peripheral nervous system. All Schwann cells are surrounded by a basal lamina. Extracellular matrix molecules in the basal lamina, such... (Review)
Review
Schwann cells form myelin in the peripheral nervous system. All Schwann cells are surrounded by a basal lamina. Extracellular matrix molecules in the basal lamina, such as laminin, regulate key aspects of Schwann cell development including the formation, architecture and function of myelin. Recent genetic and cell biological experiments suggest that Schwann cells regulate the basal lamina and its receptors in both time and space, resulting in differential functions. These findings have important implications for diseases resulting from laminin dysfunction, such as congenital muscular dystrophy 1A.
Topics: Animals; Basement Membrane; Collagen; Extracellular Matrix; Humans; Laminin; Myelin Sheath; Peripheral Nervous System; Receptors, Cell Surface; Schwann Cells
PubMed: 16956757
DOI: 10.1016/j.conb.2006.08.005 -
Journal of Neurocytology 2003Fast chemical synapses are comprised of presynaptic and postsynaptic specializations precisely aligned across a protein-filled synaptic cleft. At the vertebrate... (Review)
Review
Fast chemical synapses are comprised of presynaptic and postsynaptic specializations precisely aligned across a protein-filled synaptic cleft. At the vertebrate neuromuscular junction (NMJ), the synaptic cleft contains a structured form of extracellular matrix known as a basal lamina (BL). Synaptic BL is molecularly differentiated from the BL that covers the extrasynaptic region of the myofiber. This review summarizes current understanding of the morphology, composition, and function of the synaptic BL at the vertebrate NMJ. Considerable evidence supports the conclusion that the synaptic BL organizes and maintains pre- and postsynaptic specializations during development and regeneration, and promotes robust neurotransmission in the adult.
Topics: Animals; Basement Membrane; Humans; Membrane Proteins; Neuromuscular Junction; Synapses
PubMed: 15034274
DOI: 10.1023/B:NEUR.0000020630.74955.19 -
Progress in Brain Research 1990
Review
Topics: Animals; Basement Membrane; Muscles; Neuromuscular Junction; Receptors, Cholinergic; Regeneration
PubMed: 2267319
DOI: 10.1016/s0079-6123(08)60890-0 -
The Journal of Biological Chemistry Apr 2003
Review
Topics: Animals; Basement Membrane; Cell Differentiation; Extracellular Matrix; Humans; Muscle Contraction; Muscle Fibers, Skeletal; Muscle, Skeletal
PubMed: 12556454
DOI: 10.1074/jbc.R200027200 -
Annual Review of Neuroscience 1986The availability of several methods for the preparation of SCs free of other cell types has allowed recent experimentation providing new insights into the capacity of... (Review)
Review
The availability of several methods for the preparation of SCs free of other cell types has allowed recent experimentation providing new insights into the capacity of SCs to synthesize, release, and organize extracellular matrix materials, particularly those of the basal lamina. When these SC populations are combined in tissue culture with pure populations of neurons capable of directing SC function (without fibroblasts), new aspects of interrelationships between these cell types have come to light. In this brief chapter we review the results from this experimental approach during the last decade, and suggest the implications these observations have for interpreting known differences in SC functional expression in various body regions as well as for understanding certain disease processes. Of particular note is the discovery of an apparently essential linkage between the function of the SCs in organizing and relating to basal lamina and their ability to ensheathe and myelinate axons. It now appears that SC functional expression requires an alliance not only with the nerve fiber but also with the ECM through the production and organization of a basal lamina.
Topics: Animals; Axons; Basement Membrane; Cell Communication; Cells, Cultured; Collagen; Electrophoresis, Polyacrylamide Gel; Extracellular Matrix; Laminin; Mice; Molecular Weight; Muscular Dystrophy, Animal; Myelin Sheath; Proteins; Schwann Cells
PubMed: 3518587
DOI: 10.1146/annurev.ne.09.030186.001513 -
Developmental Neuroscience 1989
Review
Topics: Animals; Basement Membrane; Microscopy, Electron; Neuromuscular Junction; Receptor Aggregation; Receptors, Cholinergic
PubMed: 2676454
DOI: 10.1159/000111903