Is SPARC an Evolutionarily Conserved Collagen Chaperone?
Bibliographic record
Abstract
The construction of collagen fiber scaffolds, which provide the structural integrity of the extracellular matrix of connective tissues and basement membranes, is initiated by a complex mechanism of protein-folding, whereby pro-collagen alpha-chains are assembled into triple-helical procollagen molecules. This unique assembly of the procollagen molecules is guided by several endoplasmic reticulum resident molecular chaperones, including HSP47, which dissociates from procollagen molecules prior to their transport from the endoplasmic reticulum into the cis-Golgi network. SPARC, an evolutionarily conserved collagen-binding glycoprotein, which is frequently co-expressed with collagen in rapidly remodeling tissues, binds to the triple-helical region of procollagen molecules. Analysis of data from genome projects indicates that specific amino acids and sequences in SPARC that are critical for collagen binding are evolutionarily conserved in organisms ranging from nematodes to mammals. Studies of invertebrates, which do not encode HSP47, indicate that SPARC expression is required for the deposition of collagen IV in basal lamina during embryonic development. In mammals, defects in collagen deposition have been observed in normal and wound-healing tissues in the absence of SPARC expression. Based on these and other observations, we propose that intracellular SPARC acts as a collagen molecular chaperone in the endoplasmic reticulum, and that in higher organisms, SPARC acts in concert with HSP47 to ensure that only correctly folded procollagen molecules exit the endoplasmic reticulum. In contrast to HSP47, SPARC is transported from the endoplasmic reticulum through the Golgi network and into secretory vesicles for exocytosis at the plasma membrane. Hence, SPARC may also play a role in regulating post-endoplasmic reticulum events that promote collagen fibrillogenesis.
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How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.001 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.001 |
| Scholarly communication | 0.001 | 0.001 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.001 | 0.000 |
| Insufficient payload (model declined to judge) | 0.001 | 0.001 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".